Zinc in PDB 1gyt: E. Coli Aminopeptidase A (Pepa)
Enzymatic activity of E. Coli Aminopeptidase A (Pepa)
All present enzymatic activity of E. Coli Aminopeptidase A (Pepa):
3.4.11.1;
Protein crystallography data
The structure of E. Coli Aminopeptidase A (Pepa), PDB code: 1gyt
was solved by
N.Straeter,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
30.00 /
2.50
|
Space group
|
P 32
|
Cell size a, b, c (Å), α, β, γ (°)
|
178.000,
178.000,
244.400,
90.00,
90.00,
120.00
|
R / Rfree (%)
|
16.5 /
20.9
|
Other elements in 1gyt:
The structure of E. Coli Aminopeptidase A (Pepa) also contains other interesting chemical elements:
Zinc Binding Sites:
Pages:
>>> Page 1 <<<
Page 2, Binding sites: 11 -
20;
Page 3, Binding sites: 21 -
24;
Binding sites:
The binding sites of Zinc atom in the E. Coli Aminopeptidase A (Pepa)
(pdb code 1gyt). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total 24 binding sites of Zinc where determined in the
E. Coli Aminopeptidase A (Pepa), PDB code: 1gyt:
Jump to Zinc binding site number:
1;
2;
3;
4;
5;
6;
7;
8;
9;
10;
Zinc binding site 1 out
of 24 in 1gyt
Go back to
Zinc Binding Sites List in 1gyt
Zinc binding site 1 out
of 24 in the E. Coli Aminopeptidase A (Pepa)
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 1 of E. Coli Aminopeptidase A (Pepa) within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn601
b:18.1
occ:1.00
|
OD2
|
A:ASP293
|
1.9
|
13.7
|
1.0
|
O
|
A:HOH760
|
2.1
|
11.2
|
1.0
|
OE2
|
A:GLU354
|
2.1
|
5.3
|
1.0
|
NZ
|
A:LYS270
|
2.2
|
16.9
|
1.0
|
OD2
|
A:ASP275
|
2.5
|
12.3
|
1.0
|
CG
|
A:ASP293
|
2.8
|
12.3
|
1.0
|
ZN
|
A:ZN602
|
3.0
|
15.9
|
1.0
|
OD1
|
A:ASP293
|
3.0
|
11.1
|
1.0
|
CE
|
A:LYS270
|
3.1
|
11.7
|
1.0
|
CD
|
A:GLU354
|
3.1
|
9.2
|
1.0
|
OE1
|
A:GLU354
|
3.4
|
11.9
|
1.0
|
CG
|
A:ASP275
|
3.4
|
11.7
|
1.0
|
O2
|
A:CO3603
|
3.7
|
17.6
|
1.0
|
O
|
A:HOH898
|
3.8
|
13.8
|
1.0
|
CB
|
A:ASP275
|
4.0
|
10.6
|
1.0
|
CB
|
A:ASP293
|
4.3
|
13.9
|
1.0
|
O
|
A:THR379
|
4.3
|
14.2
|
1.0
|
OD1
|
A:ASP275
|
4.3
|
9.1
|
1.0
|
CG
|
A:LEU272
|
4.4
|
10.2
|
1.0
|
N
|
A:GLY355
|
4.4
|
9.2
|
1.0
|
CD
|
A:LYS270
|
4.5
|
11.3
|
1.0
|
CG
|
A:GLU354
|
4.5
|
8.7
|
1.0
|
O
|
A:ASP352
|
4.5
|
14.9
|
1.0
|
O
|
A:HOH860
|
4.5
|
22.0
|
1.0
|
CB
|
A:LEU272
|
4.6
|
12.4
|
1.0
|
CA
|
A:GLY355
|
4.7
|
9.7
|
1.0
|
OD1
|
A:ASP352
|
4.8
|
10.3
|
1.0
|
C
|
A:CO3603
|
5.0
|
16.6
|
1.0
|
|
Zinc binding site 2 out
of 24 in 1gyt
Go back to
Zinc Binding Sites List in 1gyt
Zinc binding site 2 out
of 24 in the E. Coli Aminopeptidase A (Pepa)
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 2 of E. Coli Aminopeptidase A (Pepa) within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn602
b:15.9
occ:1.00
|
O
|
A:HOH760
|
2.0
|
11.2
|
1.0
|
OE1
|
A:GLU354
|
2.0
|
11.9
|
1.0
|
OD2
|
A:ASP275
|
2.0
|
12.3
|
1.0
|
OD1
|
A:ASP352
|
2.0
|
10.3
|
1.0
|
O
|
A:ASP352
|
2.2
|
14.9
|
1.0
|
CD
|
A:GLU354
|
2.9
|
9.2
|
1.0
|
CG
|
A:ASP275
|
3.0
|
11.7
|
1.0
|
ZN
|
A:ZN601
|
3.0
|
18.1
|
1.0
|
C
|
A:ASP352
|
3.0
|
13.6
|
1.0
|
OE2
|
A:GLU354
|
3.1
|
5.3
|
1.0
|
CG
|
A:ASP352
|
3.1
|
7.7
|
1.0
|
OD1
|
A:ASP275
|
3.2
|
9.1
|
1.0
|
CA
|
A:ASP352
|
3.4
|
13.1
|
1.0
|
CB
|
A:ASP352
|
3.8
|
11.8
|
1.0
|
O
|
A:HOH898
|
4.0
|
13.8
|
1.0
|
OD2
|
A:ASP352
|
4.0
|
12.3
|
1.0
|
O2
|
A:CO3603
|
4.1
|
17.6
|
1.0
|
N
|
A:GLU354
|
4.2
|
10.0
|
1.0
|
CG
|
A:GLU354
|
4.3
|
8.7
|
1.0
|
N
|
A:ALA353
|
4.3
|
11.0
|
1.0
|
NZ
|
A:LYS282
|
4.3
|
5.9
|
1.0
|
CB
|
A:ASP275
|
4.4
|
10.6
|
1.0
|
OD2
|
A:ASP293
|
4.4
|
13.7
|
1.0
|
CE
|
A:LYS282
|
4.4
|
5.6
|
1.0
|
ND2
|
A:ASN325
|
4.5
|
16.2
|
1.0
|
CA
|
A:ALA353
|
4.7
|
10.6
|
1.0
|
N
|
A:ASP352
|
4.7
|
13.2
|
1.0
|
CA
|
A:GLY277
|
4.7
|
11.7
|
1.0
|
NZ
|
A:LYS270
|
4.8
|
16.9
|
1.0
|
CB
|
A:GLU354
|
4.8
|
8.9
|
1.0
|
O
|
A:THR351
|
4.8
|
16.4
|
1.0
|
|
Zinc binding site 3 out
of 24 in 1gyt
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Zinc Binding Sites List in 1gyt
Zinc binding site 3 out
of 24 in the E. Coli Aminopeptidase A (Pepa)
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 3 of E. Coli Aminopeptidase A (Pepa) within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Zn601
b:14.1
occ:1.00
|
OD2
|
B:ASP293
|
1.9
|
14.6
|
1.0
|
O
|
B:HOH845
|
2.0
|
7.2
|
1.0
|
OE2
|
B:GLU354
|
2.0
|
13.1
|
1.0
|
NZ
|
B:LYS270
|
2.1
|
5.8
|
1.0
|
OD2
|
B:ASP275
|
2.4
|
10.4
|
1.0
|
CG
|
B:ASP293
|
2.9
|
11.2
|
1.0
|
ZN
|
B:ZN602
|
3.0
|
19.9
|
1.0
|
CD
|
B:GLU354
|
3.1
|
12.4
|
1.0
|
OD1
|
B:ASP293
|
3.1
|
10.7
|
1.0
|
CE
|
B:LYS270
|
3.1
|
2.1
|
1.0
|
OE1
|
B:GLU354
|
3.4
|
16.7
|
1.0
|
CG
|
B:ASP275
|
3.4
|
9.7
|
1.0
|
O2
|
B:CO3603
|
3.7
|
12.8
|
1.0
|
O
|
B:HOH952
|
3.9
|
4.2
|
1.0
|
CB
|
B:ASP275
|
4.0
|
7.6
|
1.0
|
CB
|
B:ASP293
|
4.2
|
9.7
|
1.0
|
O
|
B:THR379
|
4.3
|
9.1
|
1.0
|
OD1
|
B:ASP275
|
4.4
|
7.8
|
1.0
|
CG
|
B:GLU354
|
4.4
|
10.4
|
1.0
|
N
|
B:GLY355
|
4.4
|
9.8
|
1.0
|
O
|
B:ASP352
|
4.5
|
8.2
|
1.0
|
CG
|
B:LEU272
|
4.5
|
7.4
|
1.0
|
CD
|
B:LYS270
|
4.5
|
4.4
|
1.0
|
O
|
B:HOH901
|
4.6
|
12.1
|
1.0
|
CB
|
B:LEU272
|
4.6
|
6.1
|
1.0
|
CA
|
B:GLY355
|
4.7
|
9.5
|
1.0
|
OD1
|
B:ASP352
|
4.8
|
5.3
|
1.0
|
C
|
B:CO3603
|
4.9
|
11.0
|
1.0
|
|
Zinc binding site 4 out
of 24 in 1gyt
Go back to
Zinc Binding Sites List in 1gyt
Zinc binding site 4 out
of 24 in the E. Coli Aminopeptidase A (Pepa)
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 4 of E. Coli Aminopeptidase A (Pepa) within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Zn602
b:19.9
occ:1.00
|
OD1
|
B:ASP352
|
2.0
|
5.3
|
1.0
|
OD2
|
B:ASP275
|
2.0
|
10.4
|
1.0
|
O
|
B:HOH845
|
2.1
|
7.2
|
1.0
|
OE1
|
B:GLU354
|
2.1
|
16.7
|
1.0
|
O
|
B:ASP352
|
2.1
|
8.2
|
1.0
|
CD
|
B:GLU354
|
3.0
|
12.4
|
1.0
|
ZN
|
B:ZN601
|
3.0
|
14.1
|
1.0
|
CG
|
B:ASP275
|
3.0
|
9.7
|
1.0
|
C
|
B:ASP352
|
3.0
|
10.8
|
1.0
|
CG
|
B:ASP352
|
3.1
|
8.9
|
1.0
|
OE2
|
B:GLU354
|
3.1
|
13.1
|
1.0
|
OD1
|
B:ASP275
|
3.2
|
7.8
|
1.0
|
CA
|
B:ASP352
|
3.4
|
9.1
|
1.0
|
CB
|
B:ASP352
|
3.8
|
10.0
|
1.0
|
O
|
B:HOH952
|
3.9
|
4.2
|
1.0
|
OD2
|
B:ASP352
|
4.0
|
10.2
|
1.0
|
O2
|
B:CO3603
|
4.2
|
12.8
|
1.0
|
N
|
B:ALA353
|
4.2
|
8.6
|
1.0
|
N
|
B:GLU354
|
4.3
|
7.5
|
1.0
|
NZ
|
B:LYS282
|
4.3
|
7.4
|
1.0
|
CG
|
B:GLU354
|
4.4
|
10.4
|
1.0
|
OD2
|
B:ASP293
|
4.4
|
14.6
|
1.0
|
CE
|
B:LYS282
|
4.4
|
7.6
|
1.0
|
CB
|
B:ASP275
|
4.4
|
7.6
|
1.0
|
ND2
|
B:ASN325
|
4.5
|
8.6
|
1.0
|
CA
|
B:ALA353
|
4.7
|
7.5
|
1.0
|
CA
|
B:GLY277
|
4.7
|
12.5
|
1.0
|
NZ
|
B:LYS270
|
4.8
|
5.8
|
1.0
|
N
|
B:ASP352
|
4.8
|
9.6
|
1.0
|
O
|
B:THR351
|
4.9
|
9.1
|
1.0
|
CB
|
B:GLU354
|
4.9
|
9.3
|
1.0
|
|
Zinc binding site 5 out
of 24 in 1gyt
Go back to
Zinc Binding Sites List in 1gyt
Zinc binding site 5 out
of 24 in the E. Coli Aminopeptidase A (Pepa)
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 5 of E. Coli Aminopeptidase A (Pepa) within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Zn601
b:15.1
occ:1.00
|
OD2
|
C:ASP293
|
1.9
|
11.7
|
1.0
|
O
|
C:HOH764
|
1.9
|
11.3
|
1.0
|
NZ
|
C:LYS270
|
2.2
|
9.1
|
1.0
|
OE2
|
C:GLU354
|
2.3
|
5.7
|
1.0
|
OD2
|
C:ASP275
|
2.6
|
11.7
|
1.0
|
CG
|
C:ASP293
|
2.8
|
11.4
|
1.0
|
CE
|
C:LYS270
|
2.9
|
9.1
|
1.0
|
ZN
|
C:ZN602
|
3.0
|
12.0
|
1.0
|
OD1
|
C:ASP293
|
3.1
|
8.4
|
1.0
|
CD
|
C:GLU354
|
3.2
|
9.3
|
1.0
|
OE1
|
C:GLU354
|
3.4
|
10.7
|
1.0
|
O2
|
C:CO3603
|
3.4
|
10.8
|
1.0
|
CG
|
C:ASP275
|
3.5
|
7.8
|
1.0
|
O
|
C:HOH944
|
3.8
|
9.0
|
1.0
|
CB
|
C:ASP275
|
4.0
|
5.8
|
1.0
|
O
|
C:THR379
|
4.2
|
7.3
|
1.0
|
CB
|
C:ASP293
|
4.3
|
9.6
|
1.0
|
OD1
|
C:ASP275
|
4.4
|
6.5
|
1.0
|
CD
|
C:LYS270
|
4.4
|
10.2
|
1.0
|
CG
|
C:LEU272
|
4.5
|
7.8
|
1.0
|
N
|
C:GLY355
|
4.5
|
10.1
|
1.0
|
O
|
C:ASP352
|
4.5
|
12.7
|
1.0
|
CB
|
C:LEU272
|
4.6
|
9.0
|
1.0
|
CG
|
C:GLU354
|
4.6
|
7.4
|
1.0
|
C
|
C:CO3603
|
4.7
|
11.2
|
1.0
|
O
|
C:HOH919
|
4.8
|
12.1
|
1.0
|
CA
|
C:GLY355
|
4.8
|
13.2
|
1.0
|
OD1
|
C:ASP352
|
4.9
|
9.3
|
1.0
|
|
Zinc binding site 6 out
of 24 in 1gyt
Go back to
Zinc Binding Sites List in 1gyt
Zinc binding site 6 out
of 24 in the E. Coli Aminopeptidase A (Pepa)
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 6 of E. Coli Aminopeptidase A (Pepa) within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Zn602
b:12.0
occ:1.00
|
O
|
C:HOH764
|
1.9
|
11.3
|
1.0
|
OD2
|
C:ASP275
|
2.1
|
11.7
|
1.0
|
OD1
|
C:ASP352
|
2.1
|
9.3
|
1.0
|
O
|
C:ASP352
|
2.1
|
12.7
|
1.0
|
OE1
|
C:GLU354
|
2.1
|
10.7
|
1.0
|
CG
|
C:ASP275
|
3.0
|
7.8
|
1.0
|
ZN
|
C:ZN601
|
3.0
|
15.1
|
1.0
|
C
|
C:ASP352
|
3.0
|
11.8
|
1.0
|
CD
|
C:GLU354
|
3.1
|
9.3
|
1.0
|
CG
|
C:ASP352
|
3.2
|
10.2
|
1.0
|
OD1
|
C:ASP275
|
3.2
|
6.5
|
1.0
|
OE2
|
C:GLU354
|
3.4
|
5.7
|
1.0
|
CA
|
C:ASP352
|
3.4
|
9.8
|
1.0
|
O
|
C:HOH944
|
3.8
|
9.0
|
1.0
|
CB
|
C:ASP352
|
3.9
|
9.3
|
1.0
|
O2
|
C:CO3603
|
4.1
|
10.8
|
1.0
|
OD2
|
C:ASP352
|
4.1
|
7.4
|
1.0
|
NZ
|
C:LYS282
|
4.2
|
4.3
|
1.0
|
N
|
C:ALA353
|
4.2
|
11.2
|
1.0
|
N
|
C:GLU354
|
4.2
|
9.8
|
1.0
|
CE
|
C:LYS282
|
4.2
|
2.3
|
1.0
|
OD2
|
C:ASP293
|
4.3
|
11.7
|
1.0
|
CB
|
C:ASP275
|
4.3
|
5.8
|
1.0
|
CG
|
C:GLU354
|
4.5
|
7.4
|
1.0
|
ND2
|
C:ASN325
|
4.5
|
10.2
|
1.0
|
CA
|
C:ALA353
|
4.6
|
11.2
|
1.0
|
N
|
C:ASP352
|
4.8
|
11.4
|
1.0
|
NZ
|
C:LYS270
|
4.8
|
9.1
|
1.0
|
CA
|
C:GLY277
|
4.8
|
14.1
|
1.0
|
O
|
C:THR351
|
4.9
|
11.1
|
1.0
|
C
|
C:CO3603
|
4.9
|
11.2
|
1.0
|
C
|
C:ALA353
|
5.0
|
10.9
|
1.0
|
|
Zinc binding site 7 out
of 24 in 1gyt
Go back to
Zinc Binding Sites List in 1gyt
Zinc binding site 7 out
of 24 in the E. Coli Aminopeptidase A (Pepa)
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 7 of E. Coli Aminopeptidase A (Pepa) within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Zn601
b:13.2
occ:1.00
|
OD2
|
D:ASP293
|
2.0
|
16.9
|
1.0
|
NZ
|
D:LYS270
|
2.1
|
16.7
|
1.0
|
OE2
|
D:GLU354
|
2.1
|
5.9
|
1.0
|
O
|
D:HOH826
|
2.1
|
8.6
|
1.0
|
OD2
|
D:ASP275
|
2.3
|
17.4
|
1.0
|
CE
|
D:LYS270
|
2.8
|
14.6
|
1.0
|
CG
|
D:ASP293
|
2.9
|
15.4
|
1.0
|
ZN
|
D:ZN602
|
3.0
|
15.6
|
1.0
|
OD1
|
D:ASP293
|
3.0
|
13.8
|
1.0
|
CD
|
D:GLU354
|
3.1
|
10.0
|
1.0
|
CG
|
D:ASP275
|
3.4
|
15.4
|
1.0
|
OE1
|
D:GLU354
|
3.4
|
9.0
|
1.0
|
O2
|
D:CO3603
|
3.5
|
17.1
|
1.0
|
O
|
D:HOH887
|
3.9
|
6.0
|
1.0
|
CB
|
D:ASP275
|
4.0
|
13.4
|
1.0
|
CD
|
D:LYS270
|
4.3
|
12.0
|
1.0
|
O
|
D:THR379
|
4.3
|
12.1
|
1.0
|
OD1
|
D:ASP275
|
4.3
|
13.3
|
1.0
|
CB
|
D:ASP293
|
4.3
|
13.2
|
1.0
|
CG
|
D:LEU272
|
4.4
|
10.4
|
1.0
|
CG
|
D:GLU354
|
4.4
|
11.6
|
1.0
|
O
|
D:ASP352
|
4.5
|
10.7
|
1.0
|
N
|
D:GLY355
|
4.5
|
12.3
|
1.0
|
CB
|
D:LEU272
|
4.6
|
13.1
|
1.0
|
O
|
D:HOH913
|
4.6
|
23.6
|
1.0
|
OD1
|
D:ASP352
|
4.7
|
16.5
|
1.0
|
CA
|
D:GLY355
|
4.8
|
12.1
|
1.0
|
C
|
D:CO3603
|
4.8
|
15.4
|
1.0
|
|
Zinc binding site 8 out
of 24 in 1gyt
Go back to
Zinc Binding Sites List in 1gyt
Zinc binding site 8 out
of 24 in the E. Coli Aminopeptidase A (Pepa)
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 8 of E. Coli Aminopeptidase A (Pepa) within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Zn602
b:15.6
occ:1.00
|
O
|
D:HOH826
|
2.0
|
8.6
|
1.0
|
OD1
|
D:ASP352
|
2.0
|
16.5
|
1.0
|
OE1
|
D:GLU354
|
2.1
|
9.0
|
1.0
|
O
|
D:ASP352
|
2.1
|
10.7
|
1.0
|
OD2
|
D:ASP275
|
2.2
|
17.4
|
1.0
|
CD
|
D:GLU354
|
2.9
|
10.0
|
1.0
|
C
|
D:ASP352
|
2.9
|
12.3
|
1.0
|
ZN
|
D:ZN601
|
3.0
|
13.2
|
1.0
|
CG
|
D:ASP275
|
3.0
|
15.4
|
1.0
|
OD1
|
D:ASP275
|
3.1
|
13.3
|
1.0
|
CG
|
D:ASP352
|
3.1
|
13.6
|
1.0
|
OE2
|
D:GLU354
|
3.1
|
5.9
|
1.0
|
CA
|
D:ASP352
|
3.3
|
10.9
|
1.0
|
O
|
D:HOH887
|
3.8
|
6.0
|
1.0
|
CB
|
D:ASP352
|
3.8
|
13.8
|
1.0
|
NZ
|
D:LYS282
|
4.1
|
12.8
|
1.0
|
O2
|
D:CO3603
|
4.1
|
17.1
|
1.0
|
OD2
|
D:ASP352
|
4.1
|
13.0
|
1.0
|
N
|
D:ALA353
|
4.1
|
11.6
|
1.0
|
N
|
D:GLU354
|
4.3
|
11.7
|
1.0
|
CG
|
D:GLU354
|
4.3
|
11.6
|
1.0
|
CE
|
D:LYS282
|
4.4
|
12.3
|
1.0
|
CB
|
D:ASP275
|
4.4
|
13.4
|
1.0
|
OD2
|
D:ASP293
|
4.4
|
16.9
|
1.0
|
ND2
|
D:ASN325
|
4.5
|
12.2
|
1.0
|
CA
|
D:ALA353
|
4.6
|
11.7
|
1.0
|
NZ
|
D:LYS270
|
4.6
|
16.7
|
1.0
|
N
|
D:ASP352
|
4.7
|
11.5
|
1.0
|
CA
|
D:GLY277
|
4.8
|
13.1
|
1.0
|
CB
|
D:GLU354
|
4.8
|
13.4
|
1.0
|
O
|
D:THR351
|
4.9
|
13.3
|
1.0
|
|
Zinc binding site 9 out
of 24 in 1gyt
Go back to
Zinc Binding Sites List in 1gyt
Zinc binding site 9 out
of 24 in the E. Coli Aminopeptidase A (Pepa)
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 9 of E. Coli Aminopeptidase A (Pepa) within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
E:Zn601
b:16.7
occ:1.00
|
OD2
|
E:ASP293
|
1.8
|
13.9
|
1.0
|
O
|
E:HOH778
|
2.0
|
3.7
|
1.0
|
OE2
|
E:GLU354
|
2.1
|
13.9
|
1.0
|
NZ
|
E:LYS270
|
2.2
|
14.0
|
1.0
|
OD2
|
E:ASP275
|
2.5
|
14.6
|
1.0
|
CG
|
E:ASP293
|
2.7
|
10.9
|
1.0
|
OD1
|
E:ASP293
|
2.9
|
11.9
|
1.0
|
ZN
|
E:ZN602
|
3.0
|
16.3
|
1.0
|
CE
|
E:LYS270
|
3.0
|
11.8
|
1.0
|
CD
|
E:GLU354
|
3.1
|
14.0
|
1.0
|
OE1
|
E:GLU354
|
3.4
|
14.3
|
1.0
|
CG
|
E:ASP275
|
3.4
|
13.8
|
1.0
|
O2
|
E:CO3603
|
3.7
|
14.8
|
1.0
|
CB
|
E:ASP275
|
3.9
|
11.8
|
1.0
|
O
|
E:HOH912
|
4.0
|
1.0
|
1.0
|
CB
|
E:ASP293
|
4.2
|
9.8
|
1.0
|
O
|
E:THR379
|
4.3
|
8.9
|
1.0
|
O
|
E:HOH869
|
4.3
|
16.7
|
1.0
|
CG
|
E:LEU272
|
4.4
|
13.2
|
1.0
|
OD1
|
E:ASP275
|
4.4
|
11.9
|
1.0
|
CG
|
E:GLU354
|
4.4
|
11.6
|
1.0
|
N
|
E:GLY355
|
4.5
|
11.6
|
1.0
|
CD
|
E:LYS270
|
4.5
|
13.3
|
1.0
|
O
|
E:ASP352
|
4.5
|
8.1
|
1.0
|
CB
|
E:LEU272
|
4.6
|
11.2
|
1.0
|
OD1
|
E:ASP352
|
4.8
|
5.5
|
1.0
|
CA
|
E:GLY355
|
4.8
|
12.4
|
1.0
|
|
Zinc binding site 10 out
of 24 in 1gyt
Go back to
Zinc Binding Sites List in 1gyt
Zinc binding site 10 out
of 24 in the E. Coli Aminopeptidase A (Pepa)
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 10 of E. Coli Aminopeptidase A (Pepa) within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
E:Zn602
b:16.3
occ:1.00
|
OD1
|
E:ASP352
|
1.9
|
5.5
|
1.0
|
OE1
|
E:GLU354
|
2.0
|
14.3
|
1.0
|
O
|
E:HOH778
|
2.0
|
3.7
|
1.0
|
OD2
|
E:ASP275
|
2.0
|
14.6
|
1.0
|
O
|
E:ASP352
|
2.0
|
8.1
|
1.0
|
CD
|
E:GLU354
|
2.9
|
14.0
|
1.0
|
C
|
E:ASP352
|
3.0
|
8.3
|
1.0
|
CG
|
E:ASP275
|
3.0
|
13.8
|
1.0
|
ZN
|
E:ZN601
|
3.0
|
16.7
|
1.0
|
CG
|
E:ASP352
|
3.1
|
6.8
|
1.0
|
OE2
|
E:GLU354
|
3.1
|
13.9
|
1.0
|
OD1
|
E:ASP275
|
3.2
|
11.9
|
1.0
|
CA
|
E:ASP352
|
3.4
|
7.6
|
1.0
|
CB
|
E:ASP352
|
3.8
|
7.1
|
1.0
|
O
|
E:HOH912
|
3.9
|
1.0
|
1.0
|
OD2
|
E:ASP352
|
4.0
|
8.0
|
1.0
|
N
|
E:ALA353
|
4.1
|
6.6
|
1.0
|
O2
|
E:CO3603
|
4.1
|
14.8
|
1.0
|
NZ
|
E:LYS282
|
4.2
|
11.3
|
1.0
|
N
|
E:GLU354
|
4.2
|
10.2
|
1.0
|
CE
|
E:LYS282
|
4.3
|
11.8
|
1.0
|
OD2
|
E:ASP293
|
4.3
|
13.9
|
1.0
|
CG
|
E:GLU354
|
4.3
|
11.6
|
1.0
|
CB
|
E:ASP275
|
4.3
|
11.8
|
1.0
|
ND2
|
E:ASN325
|
4.5
|
13.3
|
1.0
|
CA
|
E:ALA353
|
4.6
|
9.6
|
1.0
|
N
|
E:ASP352
|
4.7
|
9.4
|
1.0
|
CA
|
E:GLY277
|
4.7
|
10.9
|
1.0
|
NZ
|
E:LYS270
|
4.8
|
14.0
|
1.0
|
O
|
E:THR351
|
4.8
|
11.0
|
1.0
|
CB
|
E:GLU354
|
4.9
|
11.0
|
1.0
|
|
Reference:
N.Straeter,
D.J.Sherratt,
S.D.Colloms.
X-Ray Structure of Aminopeptidase A From Escherichia Coli and A Model For the Nucleoprotein Complex in Xer Site-Specific Recombination Embo J. V. 18 4513 1999.
ISSN: ISSN 0261-4189
PubMed: 10449417
DOI: 10.1093/EMBOJ/18.16.4513
Page generated: Sun Oct 13 01:49:27 2024
|