Zinc in PDB 4zla: Bestatin Complex Structure of Leucine Aminopeptidase From Helicobacter Pylori
Enzymatic activity of Bestatin Complex Structure of Leucine Aminopeptidase From Helicobacter Pylori
All present enzymatic activity of Bestatin Complex Structure of Leucine Aminopeptidase From Helicobacter Pylori:
3.4.11.1;
3.4.11.10;
Protein crystallography data
The structure of Bestatin Complex Structure of Leucine Aminopeptidase From Helicobacter Pylori, PDB code: 4zla
was solved by
J.K.Modak,
A.Roujeinikova,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
|
Resolution Low / High (Å)
|
30.55 /
1.90
|
|
Space group
|
P 1
|
|
Cell size a, b, c (Å), α, β, γ (°)
|
99.770,
99.690,
96.780,
81.89,
60.97,
75.39
|
|
R / Rfree (%)
|
17.6 /
21.9
|
Other elements in 4zla:
The structure of Bestatin Complex Structure of Leucine Aminopeptidase From Helicobacter Pylori also contains other interesting chemical elements:
Zinc Binding Sites:
Pages:
>>> Page 1 <<<
Page 2, Binding sites: 11 -
12;
Binding sites:
The binding sites of Zinc atom in the Bestatin Complex Structure of Leucine Aminopeptidase From Helicobacter Pylori
(pdb code 4zla). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total 12 binding sites of Zinc where determined in the
Bestatin Complex Structure of Leucine Aminopeptidase From Helicobacter Pylori, PDB code: 4zla:
Jump to Zinc binding site number:
1;
2;
3;
4;
5;
6;
7;
8;
9;
10;
Zinc binding site 1 out
of 12 in 4zla
Go back to
Zinc Binding Sites List in 4zla
Zinc binding site 1 out
of 12 in the Bestatin Complex Structure of Leucine Aminopeptidase From Helicobacter Pylori
 Mono view
 Stereo pair view
|
|
A full contact list of Zinc with other atoms in the Zn binding
site number 1 of Bestatin Complex Structure of Leucine Aminopeptidase From Helicobacter Pylori within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn501
b:7.5
occ:0.80
|
OE2
|
A:GLU342
|
2.0
|
9.3
|
1.0
|
|
OD2
|
A:ASP281
|
2.0
|
10.9
|
1.0
|
|
O2
|
A:BES505
|
2.1
|
11.4
|
1.0
|
|
N2
|
A:BES505
|
2.2
|
11.1
|
1.0
|
|
NZ
|
A:LYS258
|
2.3
|
4.7
|
1.0
|
|
OD2
|
A:ASP263
|
2.3
|
10.8
|
1.0
|
|
CG
|
A:ASP281
|
2.9
|
11.6
|
1.0
|
|
C2
|
A:BES505
|
3.0
|
14.0
|
1.0
|
|
CD
|
A:GLU342
|
3.0
|
8.3
|
1.0
|
|
C1
|
A:BES505
|
3.1
|
15.3
|
1.0
|
|
CE
|
A:LYS258
|
3.1
|
6.5
|
1.0
|
|
OD1
|
A:ASP281
|
3.2
|
9.4
|
1.0
|
|
CG
|
A:ASP263
|
3.2
|
9.2
|
1.0
|
|
ZN
|
A:ZN502
|
3.3
|
18.8
|
0.6
|
|
OE1
|
A:GLU342
|
3.3
|
10.2
|
1.0
|
|
O3
|
A:BCT504
|
3.5
|
12.4
|
1.0
|
|
CB
|
A:ASP263
|
3.8
|
6.6
|
1.0
|
|
OD1
|
A:ASP263
|
4.2
|
10.1
|
1.0
|
|
C3
|
A:BES505
|
4.2
|
16.9
|
1.0
|
|
O
|
A:THR367
|
4.3
|
11.4
|
1.0
|
|
C6
|
A:BES505
|
4.3
|
12.3
|
1.0
|
|
CG
|
A:LEU260
|
4.3
|
15.2
|
1.0
|
|
CB
|
A:ASP281
|
4.3
|
6.9
|
1.0
|
|
CG
|
A:GLU342
|
4.4
|
7.9
|
1.0
|
|
O3
|
A:BES505
|
4.5
|
15.4
|
1.0
|
|
CD
|
A:LYS258
|
4.5
|
8.1
|
1.0
|
|
CB
|
A:LEU260
|
4.7
|
12.6
|
1.0
|
|
N
|
A:GLY343
|
4.8
|
4.0
|
1.0
|
|
C
|
A:BCT504
|
4.8
|
11.0
|
1.0
|
|
CD1
|
A:LEU260
|
4.9
|
14.7
|
1.0
|
|
O
|
A:HOH604
|
4.9
|
24.4
|
1.0
|
|
O
|
A:ASP340
|
5.0
|
9.5
|
1.0
|
|
Zinc binding site 2 out
of 12 in 4zla
Go back to
Zinc Binding Sites List in 4zla
Zinc binding site 2 out
of 12 in the Bestatin Complex Structure of Leucine Aminopeptidase From Helicobacter Pylori
 Mono view
 Stereo pair view
|
|
A full contact list of Zinc with other atoms in the Zn binding
site number 2 of Bestatin Complex Structure of Leucine Aminopeptidase From Helicobacter Pylori within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn502
b:18.8
occ:0.60
|
OD1
|
A:ASP340
|
2.2
|
12.3
|
1.0
|
|
OD2
|
A:ASP263
|
2.3
|
10.8
|
1.0
|
|
OE1
|
A:GLU342
|
2.3
|
10.2
|
1.0
|
|
O
|
A:ASP340
|
2.3
|
9.5
|
1.0
|
|
O2
|
A:BES505
|
2.3
|
11.4
|
1.0
|
|
O3
|
A:BES505
|
2.5
|
15.4
|
1.0
|
|
C3
|
A:BES505
|
3.0
|
16.9
|
1.0
|
|
CG
|
A:ASP263
|
3.1
|
9.2
|
1.0
|
|
C2
|
A:BES505
|
3.1
|
14.0
|
1.0
|
|
CG
|
A:ASP340
|
3.1
|
13.3
|
1.0
|
|
OD1
|
A:ASP263
|
3.2
|
10.1
|
1.0
|
|
C
|
A:ASP340
|
3.2
|
9.3
|
1.0
|
|
CD
|
A:GLU342
|
3.2
|
8.3
|
1.0
|
|
ZN
|
A:ZN501
|
3.3
|
7.5
|
0.8
|
|
CA
|
A:ASP340
|
3.5
|
8.2
|
1.0
|
|
OE2
|
A:GLU342
|
3.5
|
9.3
|
1.0
|
|
NZ
|
A:LYS270
|
3.8
|
12.6
|
1.0
|
|
C1
|
A:BES505
|
3.8
|
15.3
|
1.0
|
|
CB
|
A:ASP340
|
3.9
|
8.7
|
1.0
|
|
CE
|
A:LYS270
|
3.9
|
10.8
|
1.0
|
|
OD2
|
A:ASP340
|
4.0
|
14.3
|
1.0
|
|
O3
|
A:BCT504
|
4.1
|
12.4
|
1.0
|
|
N2
|
A:BES505
|
4.2
|
11.1
|
1.0
|
|
N1
|
A:BES505
|
4.3
|
20.1
|
1.0
|
|
N
|
A:ALA341
|
4.3
|
8.3
|
1.0
|
|
ND2
|
A:ASN313
|
4.4
|
6.3
|
1.0
|
|
N
|
A:GLU342
|
4.5
|
7.7
|
1.0
|
|
CB
|
A:ASP263
|
4.5
|
6.6
|
1.0
|
|
CG
|
A:GLU342
|
4.6
|
7.9
|
1.0
|
|
CA
|
A:GLY265
|
4.7
|
6.6
|
1.0
|
|
CA
|
A:ALA341
|
4.8
|
5.9
|
1.0
|
|
C
|
A:BCT504
|
4.9
|
11.0
|
1.0
|
|
N
|
A:ASP340
|
4.9
|
6.3
|
1.0
|
|
O1
|
A:BCT504
|
4.9
|
25.9
|
1.0
|
|
C4
|
A:BES505
|
5.0
|
25.8
|
1.0
|
|
OD2
|
A:ASP281
|
5.0
|
10.9
|
1.0
|
|
CB
|
A:GLU342
|
5.0
|
5.8
|
1.0
|
|
Zinc binding site 3 out
of 12 in 4zla
Go back to
Zinc Binding Sites List in 4zla
Zinc binding site 3 out
of 12 in the Bestatin Complex Structure of Leucine Aminopeptidase From Helicobacter Pylori
 Mono view
 Stereo pair view
|
|
A full contact list of Zinc with other atoms in the Zn binding
site number 3 of Bestatin Complex Structure of Leucine Aminopeptidase From Helicobacter Pylori within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Zn501
b:9.7
occ:0.90
|
OD2
|
B:ASP281
|
2.0
|
9.3
|
1.0
|
|
O2
|
B:BES505
|
2.0
|
12.2
|
1.0
|
|
OE2
|
B:GLU342
|
2.1
|
10.5
|
1.0
|
|
NZ
|
B:LYS258
|
2.2
|
10.8
|
1.0
|
|
N2
|
B:BES505
|
2.2
|
16.5
|
1.0
|
|
OD2
|
B:ASP263
|
2.3
|
12.3
|
1.0
|
|
CG
|
B:ASP281
|
2.9
|
10.3
|
1.0
|
|
C2
|
B:BES505
|
3.0
|
11.1
|
1.0
|
|
C1
|
B:BES505
|
3.1
|
15.8
|
1.0
|
|
CE
|
B:LYS258
|
3.1
|
7.7
|
1.0
|
|
CD
|
B:GLU342
|
3.1
|
10.2
|
1.0
|
|
OD1
|
B:ASP281
|
3.2
|
8.6
|
1.0
|
|
ZN
|
B:ZN502
|
3.2
|
20.0
|
0.6
|
|
CG
|
B:ASP263
|
3.3
|
6.8
|
1.0
|
|
OE1
|
B:GLU342
|
3.3
|
9.8
|
1.0
|
|
O3
|
B:BCT504
|
3.6
|
10.8
|
1.0
|
|
CB
|
B:ASP263
|
3.8
|
12.1
|
1.0
|
|
C3
|
B:BES505
|
4.2
|
11.9
|
1.0
|
|
OD1
|
B:ASP263
|
4.2
|
8.2
|
1.0
|
|
O
|
B:THR367
|
4.3
|
9.8
|
1.0
|
|
CB
|
B:ASP281
|
4.3
|
5.5
|
1.0
|
|
C6
|
B:BES505
|
4.3
|
13.6
|
1.0
|
|
CG
|
B:GLU342
|
4.5
|
8.6
|
1.0
|
|
CD
|
B:LYS258
|
4.5
|
5.9
|
1.0
|
|
O3
|
B:BES505
|
4.5
|
14.0
|
1.0
|
|
CG
|
B:LEU260
|
4.6
|
10.9
|
1.0
|
|
N
|
B:GLY343
|
4.7
|
4.5
|
1.0
|
|
CB
|
B:LEU260
|
4.8
|
10.3
|
1.0
|
|
C
|
B:BCT504
|
5.0
|
9.8
|
1.0
|
|
O
|
B:ASP340
|
5.0
|
10.0
|
1.0
|
|
Zinc binding site 4 out
of 12 in 4zla
Go back to
Zinc Binding Sites List in 4zla
Zinc binding site 4 out
of 12 in the Bestatin Complex Structure of Leucine Aminopeptidase From Helicobacter Pylori
 Mono view
 Stereo pair view
|
|
A full contact list of Zinc with other atoms in the Zn binding
site number 4 of Bestatin Complex Structure of Leucine Aminopeptidase From Helicobacter Pylori within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Zn502
b:20.0
occ:0.60
|
OD1
|
B:ASP340
|
2.2
|
10.6
|
1.0
|
|
OE1
|
B:GLU342
|
2.2
|
9.8
|
1.0
|
|
O2
|
B:BES505
|
2.3
|
12.2
|
1.0
|
|
OD2
|
B:ASP263
|
2.3
|
12.3
|
1.0
|
|
O
|
B:ASP340
|
2.3
|
10.0
|
1.0
|
|
O3
|
B:BES505
|
2.6
|
14.0
|
1.0
|
|
C3
|
B:BES505
|
3.0
|
11.9
|
1.0
|
|
CG
|
B:ASP263
|
3.1
|
6.8
|
1.0
|
|
C2
|
B:BES505
|
3.1
|
11.1
|
1.0
|
|
OD1
|
B:ASP263
|
3.1
|
8.2
|
1.0
|
|
CG
|
B:ASP340
|
3.2
|
11.9
|
1.0
|
|
CD
|
B:GLU342
|
3.2
|
10.2
|
1.0
|
|
C
|
B:ASP340
|
3.2
|
9.4
|
1.0
|
|
ZN
|
B:ZN501
|
3.2
|
9.7
|
0.9
|
|
OE2
|
B:GLU342
|
3.4
|
10.5
|
1.0
|
|
CA
|
B:ASP340
|
3.5
|
8.1
|
1.0
|
|
NZ
|
B:LYS270
|
3.7
|
12.0
|
1.0
|
|
C1
|
B:BES505
|
3.8
|
15.8
|
1.0
|
|
CB
|
B:ASP340
|
3.9
|
9.5
|
1.0
|
|
CE
|
B:LYS270
|
3.9
|
12.0
|
1.0
|
|
OD2
|
B:ASP340
|
4.0
|
12.8
|
1.0
|
|
O3
|
B:BCT504
|
4.1
|
10.8
|
1.0
|
|
N2
|
B:BES505
|
4.1
|
16.5
|
1.0
|
|
N1
|
B:BES505
|
4.2
|
13.3
|
1.0
|
|
N
|
B:ALA341
|
4.4
|
7.5
|
1.0
|
|
ND2
|
B:ASN313
|
4.4
|
7.9
|
1.0
|
|
N
|
B:GLU342
|
4.4
|
6.1
|
1.0
|
|
CB
|
B:ASP263
|
4.5
|
12.1
|
1.0
|
|
CG
|
B:GLU342
|
4.6
|
8.6
|
1.0
|
|
CA
|
B:GLY265
|
4.7
|
8.2
|
1.0
|
|
CA
|
B:ALA341
|
4.8
|
7.2
|
1.0
|
|
OD2
|
B:ASP281
|
4.8
|
9.3
|
1.0
|
|
N
|
B:ASP340
|
4.9
|
5.8
|
1.0
|
|
C4
|
B:BES505
|
4.9
|
20.2
|
1.0
|
|
C
|
B:BCT504
|
4.9
|
9.8
|
1.0
|
|
O1
|
B:BCT504
|
5.0
|
29.3
|
1.0
|
|
CB
|
B:GLU342
|
5.0
|
8.9
|
1.0
|
|
Zinc binding site 5 out
of 12 in 4zla
Go back to
Zinc Binding Sites List in 4zla
Zinc binding site 5 out
of 12 in the Bestatin Complex Structure of Leucine Aminopeptidase From Helicobacter Pylori
 Mono view
 Stereo pair view
|
|
A full contact list of Zinc with other atoms in the Zn binding
site number 5 of Bestatin Complex Structure of Leucine Aminopeptidase From Helicobacter Pylori within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Zn501
b:11.0
occ:0.80
|
OE2
|
C:GLU342
|
2.1
|
9.4
|
1.0
|
|
OD2
|
C:ASP281
|
2.1
|
11.8
|
1.0
|
|
O2
|
C:BES505
|
2.2
|
11.8
|
1.0
|
|
N2
|
C:BES505
|
2.2
|
13.7
|
1.0
|
|
NZ
|
C:LYS258
|
2.4
|
8.6
|
1.0
|
|
OD2
|
C:ASP263
|
2.4
|
11.9
|
1.0
|
|
CG
|
C:ASP281
|
2.9
|
10.8
|
1.0
|
|
C2
|
C:BES505
|
3.0
|
13.2
|
1.0
|
|
C1
|
C:BES505
|
3.1
|
16.9
|
1.0
|
|
CD
|
C:GLU342
|
3.1
|
11.0
|
1.0
|
|
CE
|
C:LYS258
|
3.1
|
10.3
|
1.0
|
|
OD1
|
C:ASP281
|
3.1
|
10.7
|
1.0
|
|
ZN
|
C:ZN502
|
3.3
|
20.4
|
0.6
|
|
CG
|
C:ASP263
|
3.3
|
14.3
|
1.0
|
|
OE1
|
C:GLU342
|
3.4
|
9.4
|
1.0
|
|
O1
|
C:BCT504
|
3.6
|
13.1
|
1.0
|
|
CB
|
C:ASP263
|
3.8
|
12.2
|
1.0
|
|
C6
|
C:BES505
|
4.3
|
14.8
|
1.0
|
|
C3
|
C:BES505
|
4.3
|
13.0
|
1.0
|
|
OD1
|
C:ASP263
|
4.3
|
8.5
|
1.0
|
|
O
|
C:THR367
|
4.3
|
11.2
|
1.0
|
|
CB
|
C:ASP281
|
4.3
|
9.5
|
1.0
|
|
CG
|
C:GLU342
|
4.5
|
8.9
|
1.0
|
|
O3
|
C:BES505
|
4.5
|
15.3
|
1.0
|
|
CD
|
C:LYS258
|
4.6
|
10.2
|
1.0
|
|
CG
|
C:LEU260
|
4.6
|
14.5
|
1.0
|
|
CB
|
C:LEU260
|
4.7
|
13.3
|
1.0
|
|
N
|
C:GLY343
|
4.7
|
5.9
|
1.0
|
|
C
|
C:BCT504
|
4.9
|
10.2
|
1.0
|
|
CA
|
C:GLY343
|
5.0
|
8.6
|
1.0
|
|
O
|
C:ASP340
|
5.0
|
9.6
|
1.0
|
|
Zinc binding site 6 out
of 12 in 4zla
Go back to
Zinc Binding Sites List in 4zla
Zinc binding site 6 out
of 12 in the Bestatin Complex Structure of Leucine Aminopeptidase From Helicobacter Pylori
 Mono view
 Stereo pair view
|
|
A full contact list of Zinc with other atoms in the Zn binding
site number 6 of Bestatin Complex Structure of Leucine Aminopeptidase From Helicobacter Pylori within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Zn502
b:20.4
occ:0.60
|
OD1
|
C:ASP340
|
2.1
|
12.3
|
1.0
|
|
OE1
|
C:GLU342
|
2.3
|
9.4
|
1.0
|
|
O2
|
C:BES505
|
2.3
|
11.8
|
1.0
|
|
OD2
|
C:ASP263
|
2.3
|
11.9
|
1.0
|
|
O
|
C:ASP340
|
2.4
|
9.6
|
1.0
|
|
O3
|
C:BES505
|
2.6
|
15.3
|
1.0
|
|
C3
|
C:BES505
|
3.0
|
13.0
|
1.0
|
|
CG
|
C:ASP263
|
3.1
|
14.3
|
1.0
|
|
CG
|
C:ASP340
|
3.1
|
15.4
|
1.0
|
|
C2
|
C:BES505
|
3.1
|
13.2
|
1.0
|
|
OD1
|
C:ASP263
|
3.2
|
8.5
|
1.0
|
|
CD
|
C:GLU342
|
3.2
|
11.0
|
1.0
|
|
C
|
C:ASP340
|
3.2
|
11.2
|
1.0
|
|
ZN
|
C:ZN501
|
3.3
|
11.0
|
0.8
|
|
OE2
|
C:GLU342
|
3.5
|
9.4
|
1.0
|
|
CA
|
C:ASP340
|
3.5
|
10.3
|
1.0
|
|
NZ
|
C:LYS270
|
3.7
|
11.6
|
1.0
|
|
C1
|
C:BES505
|
3.8
|
16.9
|
1.0
|
|
CE
|
C:LYS270
|
3.9
|
14.1
|
1.0
|
|
CB
|
C:ASP340
|
3.9
|
9.9
|
1.0
|
|
OD2
|
C:ASP340
|
3.9
|
13.0
|
1.0
|
|
N2
|
C:BES505
|
4.0
|
13.7
|
1.0
|
|
O1
|
C:BCT504
|
4.1
|
13.1
|
1.0
|
|
N1
|
C:BES505
|
4.2
|
14.9
|
1.0
|
|
N
|
C:ALA341
|
4.4
|
8.1
|
1.0
|
|
ND2
|
C:ASN313
|
4.4
|
7.4
|
1.0
|
|
N
|
C:GLU342
|
4.5
|
6.5
|
1.0
|
|
CB
|
C:ASP263
|
4.5
|
12.2
|
1.0
|
|
CG
|
C:GLU342
|
4.6
|
8.9
|
1.0
|
|
CA
|
C:GLY265
|
4.8
|
8.9
|
1.0
|
|
CA
|
C:ALA341
|
4.9
|
7.3
|
1.0
|
|
N
|
C:ASP340
|
4.9
|
7.7
|
1.0
|
|
C
|
C:BCT504
|
4.9
|
10.2
|
1.0
|
|
C4
|
C:BES505
|
5.0
|
23.1
|
1.0
|
|
OD2
|
C:ASP281
|
5.0
|
11.8
|
1.0
|
|
Zinc binding site 7 out
of 12 in 4zla
Go back to
Zinc Binding Sites List in 4zla
Zinc binding site 7 out
of 12 in the Bestatin Complex Structure of Leucine Aminopeptidase From Helicobacter Pylori
 Mono view
 Stereo pair view
|
|
A full contact list of Zinc with other atoms in the Zn binding
site number 7 of Bestatin Complex Structure of Leucine Aminopeptidase From Helicobacter Pylori within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Zn501
b:7.5
occ:0.80
|
OD2
|
D:ASP281
|
2.0
|
10.8
|
1.0
|
|
OE2
|
D:GLU342
|
2.0
|
10.0
|
1.0
|
|
O2
|
D:BES505
|
2.1
|
10.4
|
1.0
|
|
NZ
|
D:LYS258
|
2.1
|
8.6
|
1.0
|
|
N2
|
D:BES505
|
2.2
|
14.7
|
1.0
|
|
OD2
|
D:ASP263
|
2.3
|
11.4
|
1.0
|
|
C2
|
D:BES505
|
2.9
|
10.2
|
1.0
|
|
CG
|
D:ASP281
|
2.9
|
9.1
|
1.0
|
|
C1
|
D:BES505
|
3.0
|
12.4
|
1.0
|
|
CD
|
D:GLU342
|
3.0
|
8.8
|
1.0
|
|
CE
|
D:LYS258
|
3.1
|
7.0
|
1.0
|
|
OD1
|
D:ASP281
|
3.2
|
10.3
|
1.0
|
|
ZN
|
D:ZN502
|
3.2
|
22.4
|
0.6
|
|
CG
|
D:ASP263
|
3.2
|
13.1
|
1.0
|
|
OE1
|
D:GLU342
|
3.3
|
11.1
|
1.0
|
|
O1
|
D:BCT504
|
3.6
|
9.1
|
1.0
|
|
CB
|
D:ASP263
|
3.8
|
8.7
|
1.0
|
|
OD1
|
D:ASP263
|
4.2
|
9.5
|
1.0
|
|
C3
|
D:BES505
|
4.2
|
12.7
|
1.0
|
|
C6
|
D:BES505
|
4.3
|
11.1
|
1.0
|
|
O
|
D:THR367
|
4.3
|
13.4
|
1.0
|
|
CB
|
D:ASP281
|
4.3
|
6.9
|
1.0
|
|
CG
|
D:GLU342
|
4.4
|
5.9
|
1.0
|
|
O3
|
D:BES505
|
4.5
|
13.5
|
1.0
|
|
CD
|
D:LYS258
|
4.5
|
7.2
|
1.0
|
|
CG
|
D:LEU260
|
4.6
|
11.8
|
1.0
|
|
N
|
D:GLY343
|
4.7
|
7.3
|
1.0
|
|
CB
|
D:LEU260
|
4.8
|
12.2
|
1.0
|
|
C
|
D:BCT504
|
4.9
|
10.2
|
1.0
|
|
Zinc binding site 8 out
of 12 in 4zla
Go back to
Zinc Binding Sites List in 4zla
Zinc binding site 8 out
of 12 in the Bestatin Complex Structure of Leucine Aminopeptidase From Helicobacter Pylori
 Mono view
 Stereo pair view
|
|
A full contact list of Zinc with other atoms in the Zn binding
site number 8 of Bestatin Complex Structure of Leucine Aminopeptidase From Helicobacter Pylori within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Zn502
b:22.4
occ:0.60
|
O2
|
D:BES505
|
2.2
|
10.4
|
1.0
|
|
OD1
|
D:ASP340
|
2.2
|
9.9
|
1.0
|
|
OE1
|
D:GLU342
|
2.3
|
11.1
|
1.0
|
|
OD2
|
D:ASP263
|
2.3
|
11.4
|
1.0
|
|
O
|
D:ASP340
|
2.4
|
8.1
|
1.0
|
|
O3
|
D:BES505
|
2.5
|
13.5
|
1.0
|
|
C3
|
D:BES505
|
2.9
|
12.7
|
1.0
|
|
C2
|
D:BES505
|
3.0
|
10.2
|
1.0
|
|
CG
|
D:ASP263
|
3.1
|
13.1
|
1.0
|
|
OD1
|
D:ASP263
|
3.1
|
9.5
|
1.0
|
|
CG
|
D:ASP340
|
3.2
|
11.7
|
1.0
|
|
CD
|
D:GLU342
|
3.2
|
8.8
|
1.0
|
|
ZN
|
D:ZN501
|
3.2
|
7.5
|
0.8
|
|
C
|
D:ASP340
|
3.2
|
10.6
|
1.0
|
|
OE2
|
D:GLU342
|
3.4
|
10.0
|
1.0
|
|
CA
|
D:ASP340
|
3.6
|
9.6
|
1.0
|
|
C1
|
D:BES505
|
3.7
|
12.4
|
1.0
|
|
NZ
|
D:LYS270
|
3.7
|
17.9
|
1.0
|
|
CE
|
D:LYS270
|
3.9
|
11.2
|
1.0
|
|
CB
|
D:ASP340
|
3.9
|
7.0
|
1.0
|
|
OD2
|
D:ASP340
|
4.0
|
11.2
|
1.0
|
|
N2
|
D:BES505
|
4.1
|
14.7
|
1.0
|
|
N1
|
D:BES505
|
4.1
|
11.5
|
1.0
|
|
O1
|
D:BCT504
|
4.2
|
9.1
|
1.0
|
|
N
|
D:ALA341
|
4.4
|
10.4
|
1.0
|
|
N
|
D:GLU342
|
4.5
|
6.8
|
1.0
|
|
CB
|
D:ASP263
|
4.5
|
8.7
|
1.0
|
|
ND2
|
D:ASN313
|
4.5
|
5.7
|
1.0
|
|
CG
|
D:GLU342
|
4.6
|
5.9
|
1.0
|
|
CA
|
D:GLY265
|
4.7
|
8.2
|
1.0
|
|
CA
|
D:ALA341
|
4.8
|
8.7
|
1.0
|
|
OD2
|
D:ASP281
|
4.8
|
10.8
|
1.0
|
|
C4
|
D:BES505
|
4.8
|
19.0
|
1.0
|
|
O3
|
D:BCT504
|
4.9
|
24.1
|
1.0
|
|
C
|
D:BCT504
|
4.9
|
10.2
|
1.0
|
|
NZ
|
D:LYS258
|
4.9
|
8.6
|
1.0
|
|
N
|
D:ASP340
|
5.0
|
6.2
|
1.0
|
|
Zinc binding site 9 out
of 12 in 4zla
Go back to
Zinc Binding Sites List in 4zla
Zinc binding site 9 out
of 12 in the Bestatin Complex Structure of Leucine Aminopeptidase From Helicobacter Pylori
 Mono view
 Stereo pair view
|
|
A full contact list of Zinc with other atoms in the Zn binding
site number 9 of Bestatin Complex Structure of Leucine Aminopeptidase From Helicobacter Pylori within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
E:Zn501
b:13.0
occ:1.00
|
O2
|
E:BES505
|
2.0
|
9.4
|
1.0
|
|
OD2
|
E:ASP281
|
2.0
|
8.9
|
1.0
|
|
OE2
|
E:GLU342
|
2.0
|
11.3
|
1.0
|
|
N2
|
E:BES505
|
2.2
|
15.7
|
1.0
|
|
OD2
|
E:ASP263
|
2.3
|
8.7
|
1.0
|
|
NZ
|
E:LYS258
|
2.3
|
7.2
|
1.0
|
|
C2
|
E:BES505
|
2.9
|
13.4
|
1.0
|
|
CG
|
E:ASP281
|
2.9
|
9.7
|
1.0
|
|
C1
|
E:BES505
|
3.0
|
14.1
|
1.0
|
|
CD
|
E:GLU342
|
3.0
|
10.9
|
1.0
|
|
CE
|
E:LYS258
|
3.1
|
10.0
|
1.0
|
|
OD1
|
E:ASP281
|
3.2
|
12.1
|
1.0
|
|
CG
|
E:ASP263
|
3.2
|
9.5
|
1.0
|
|
ZN
|
E:ZN502
|
3.3
|
18.7
|
0.6
|
|
OE1
|
E:GLU342
|
3.3
|
11.4
|
1.0
|
|
O3
|
E:BCT504
|
3.6
|
8.4
|
1.0
|
|
CB
|
E:ASP263
|
3.7
|
8.1
|
1.0
|
|
OD1
|
E:ASP263
|
4.1
|
8.3
|
1.0
|
|
C3
|
E:BES505
|
4.2
|
14.3
|
1.0
|
|
C6
|
E:BES505
|
4.3
|
9.1
|
1.0
|
|
CB
|
E:ASP281
|
4.3
|
6.2
|
1.0
|
|
O
|
E:THR367
|
4.3
|
7.7
|
1.0
|
|
CG
|
E:GLU342
|
4.4
|
7.7
|
1.0
|
|
O3
|
E:BES505
|
4.5
|
15.0
|
1.0
|
|
CD
|
E:LYS258
|
4.6
|
6.8
|
1.0
|
|
CG
|
E:LEU260
|
4.7
|
11.8
|
1.0
|
|
N
|
E:GLY343
|
4.8
|
8.7
|
1.0
|
|
CB
|
E:LEU260
|
4.8
|
11.9
|
1.0
|
|
C
|
E:BCT504
|
4.9
|
12.3
|
1.0
|
|
O
|
E:ASP340
|
5.0
|
11.4
|
1.0
|
|
Zinc binding site 10 out
of 12 in 4zla
Go back to
Zinc Binding Sites List in 4zla
Zinc binding site 10 out
of 12 in the Bestatin Complex Structure of Leucine Aminopeptidase From Helicobacter Pylori
 Mono view
 Stereo pair view
|
|
A full contact list of Zinc with other atoms in the Zn binding
site number 10 of Bestatin Complex Structure of Leucine Aminopeptidase From Helicobacter Pylori within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
E:Zn502
b:18.7
occ:0.60
|
OD1
|
E:ASP340
|
2.2
|
11.4
|
1.0
|
|
OD2
|
E:ASP263
|
2.3
|
8.7
|
1.0
|
|
OE1
|
E:GLU342
|
2.3
|
11.4
|
1.0
|
|
O
|
E:ASP340
|
2.4
|
11.4
|
1.0
|
|
O2
|
E:BES505
|
2.4
|
9.4
|
1.0
|
|
O3
|
E:BES505
|
2.7
|
15.0
|
1.0
|
|
CG
|
E:ASP263
|
3.0
|
9.5
|
1.0
|
|
C3
|
E:BES505
|
3.0
|
14.3
|
1.0
|
|
OD1
|
E:ASP263
|
3.1
|
8.3
|
1.0
|
|
C2
|
E:BES505
|
3.1
|
13.4
|
1.0
|
|
CG
|
E:ASP340
|
3.2
|
14.0
|
1.0
|
|
CD
|
E:GLU342
|
3.2
|
10.9
|
1.0
|
|
C
|
E:ASP340
|
3.2
|
10.5
|
1.0
|
|
ZN
|
E:ZN501
|
3.3
|
13.0
|
1.0
|
|
OE2
|
E:GLU342
|
3.5
|
11.3
|
1.0
|
|
CA
|
E:ASP340
|
3.5
|
7.8
|
1.0
|
|
NZ
|
E:LYS270
|
3.8
|
14.1
|
1.0
|
|
C1
|
E:BES505
|
3.8
|
14.1
|
1.0
|
|
CB
|
E:ASP340
|
3.9
|
7.7
|
1.0
|
|
CE
|
E:LYS270
|
4.0
|
11.8
|
1.0
|
|
OD2
|
E:ASP340
|
4.0
|
15.7
|
1.0
|
|
O3
|
E:BCT504
|
4.2
|
8.4
|
1.0
|
|
N2
|
E:BES505
|
4.2
|
15.7
|
1.0
|
|
N1
|
E:BES505
|
4.3
|
17.2
|
1.0
|
|
ND2
|
E:ASN313
|
4.3
|
7.0
|
1.0
|
|
N
|
E:ALA341
|
4.4
|
9.6
|
1.0
|
|
N
|
E:GLU342
|
4.5
|
7.5
|
1.0
|
|
CB
|
E:ASP263
|
4.5
|
8.1
|
1.0
|
|
CG
|
E:GLU342
|
4.5
|
7.7
|
1.0
|
|
CA
|
E:GLY265
|
4.7
|
7.1
|
1.0
|
|
O2
|
E:BCT504
|
4.9
|
19.6
|
1.0
|
|
C
|
E:BCT504
|
4.9
|
12.3
|
1.0
|
|
OD2
|
E:ASP281
|
4.9
|
8.9
|
1.0
|
|
CA
|
E:ALA341
|
4.9
|
8.6
|
1.0
|
|
N
|
E:ASP340
|
4.9
|
6.1
|
1.0
|
|
C4
|
E:BES505
|
5.0
|
25.8
|
1.0
|
|
CB
|
E:GLU342
|
5.0
|
4.1
|
1.0
|
|
O
|
E:THR339
|
5.0
|
7.3
|
1.0
|
|
Reference:
J.K.Modak,
W.Rut,
L.C.Wijeyewickrema,
R.N.Pike,
M.Drag,
A.Roujeinikova.
Structural Basis For Substrate Specificity of Helicobacter Pylori M17 Aminopeptidase. Biochimie V. 121 60 2016.
ISSN: ISSN 0300-9084
PubMed: 26616008
DOI: 10.1016/J.BIOCHI.2015.11.021
Page generated: Wed Dec 16 05:59:30 2020
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