Zinc in PDB 5lds: Structure of the Porcine Aminopeptidase N Ectodomain
Enzymatic activity of Structure of the Porcine Aminopeptidase N Ectodomain
All present enzymatic activity of Structure of the Porcine Aminopeptidase N Ectodomain:
3.4.11.2;
Protein crystallography data
The structure of Structure of the Porcine Aminopeptidase N Ectodomain, PDB code: 5lds
was solved by
C.Santiago,
J.Reguera,
G.Mudgal,
J.M.Casasnovas,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
24.96 /
2.00
|
Space group
|
P 1
|
Cell size a, b, c (Å), α, β, γ (°)
|
78.670,
78.770,
223.870,
99.66,
92.62,
111.33
|
R / Rfree (%)
|
16.9 /
20.7
|
Zinc Binding Sites:
The binding sites of Zinc atom in the Structure of the Porcine Aminopeptidase N Ectodomain
(pdb code 5lds). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the
Structure of the Porcine Aminopeptidase N Ectodomain, PDB code: 5lds:
Jump to Zinc binding site number:
1;
2;
3;
4;
Zinc binding site 1 out
of 4 in 5lds
Go back to
Zinc Binding Sites List in 5lds
Zinc binding site 1 out
of 4 in the Structure of the Porcine Aminopeptidase N Ectodomain
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 1 of Structure of the Porcine Aminopeptidase N Ectodomain within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn1001
b:3.4
occ:1.00
|
O
|
A:ACT1017
|
1.9
|
6.0
|
1.0
|
OE1
|
A:GLU406
|
2.0
|
3.0
|
1.0
|
NE2
|
A:HIS387
|
2.0
|
3.5
|
1.0
|
NE2
|
A:HIS383
|
2.1
|
3.0
|
1.0
|
C
|
A:ACT1017
|
2.5
|
13.6
|
1.0
|
OXT
|
A:ACT1017
|
2.6
|
11.1
|
1.0
|
CD
|
A:GLU406
|
2.8
|
7.7
|
1.0
|
CD2
|
A:HIS387
|
3.0
|
2.9
|
1.0
|
CE1
|
A:HIS383
|
3.0
|
4.8
|
1.0
|
OE2
|
A:GLU406
|
3.0
|
7.8
|
1.0
|
CE1
|
A:HIS387
|
3.0
|
3.0
|
1.0
|
CD2
|
A:HIS383
|
3.1
|
6.4
|
1.0
|
O
|
A:HOH1203
|
3.4
|
6.6
|
1.0
|
CE2
|
A:TYR472
|
3.8
|
4.0
|
1.0
|
CH3
|
A:ACT1017
|
4.0
|
13.6
|
1.0
|
OH
|
A:TYR472
|
4.0
|
3.1
|
1.0
|
CB
|
A:ALA409
|
4.1
|
4.1
|
1.0
|
ND1
|
A:HIS387
|
4.1
|
3.0
|
1.0
|
ND1
|
A:HIS383
|
4.1
|
3.0
|
1.0
|
CG
|
A:HIS387
|
4.2
|
9.0
|
1.0
|
CG
|
A:HIS383
|
4.2
|
3.2
|
1.0
|
CG
|
A:GLU406
|
4.3
|
7.1
|
1.0
|
CZ
|
A:TYR472
|
4.3
|
5.2
|
1.0
|
OE1
|
A:GLU350
|
4.5
|
4.9
|
1.0
|
CA
|
A:GLU406
|
4.7
|
4.8
|
1.0
|
CB
|
A:GLU406
|
4.7
|
6.3
|
1.0
|
CD2
|
A:TYR472
|
4.7
|
4.4
|
1.0
|
OE2
|
A:GLU384
|
4.8
|
8.8
|
1.0
|
O
|
A:HOH1334
|
4.9
|
5.0
|
1.0
|
|
Zinc binding site 2 out
of 4 in 5lds
Go back to
Zinc Binding Sites List in 5lds
Zinc binding site 2 out
of 4 in the Structure of the Porcine Aminopeptidase N Ectodomain
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 2 of Structure of the Porcine Aminopeptidase N Ectodomain within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Zn1001
b:9.6
occ:1.00
|
OE1
|
B:GLU406
|
2.0
|
7.4
|
1.0
|
OXT
|
B:ACT1012
|
2.0
|
8.9
|
1.0
|
NE2
|
B:HIS383
|
2.0
|
7.4
|
1.0
|
NE2
|
B:HIS387
|
2.1
|
7.5
|
1.0
|
O
|
B:ACT1012
|
2.5
|
15.7
|
1.0
|
C
|
B:ACT1012
|
2.6
|
12.6
|
1.0
|
CD
|
B:GLU406
|
2.8
|
10.0
|
1.0
|
CE1
|
B:HIS383
|
3.0
|
7.4
|
1.0
|
CD2
|
B:HIS387
|
3.0
|
7.5
|
1.0
|
OE2
|
B:GLU406
|
3.0
|
11.3
|
1.0
|
CD2
|
B:HIS383
|
3.0
|
12.7
|
1.0
|
CE1
|
B:HIS387
|
3.1
|
7.6
|
1.0
|
O
|
B:HOH1227
|
3.7
|
10.8
|
1.0
|
CE2
|
B:TYR472
|
3.8
|
13.6
|
1.0
|
OH
|
B:TYR472
|
4.0
|
7.5
|
1.0
|
CH3
|
B:ACT1012
|
4.1
|
13.4
|
1.0
|
ND1
|
B:HIS383
|
4.1
|
7.4
|
1.0
|
CG
|
B:HIS383
|
4.2
|
7.4
|
1.0
|
CB
|
B:ALA409
|
4.2
|
15.3
|
1.0
|
CG
|
B:HIS387
|
4.2
|
11.3
|
1.0
|
ND1
|
B:HIS387
|
4.2
|
7.7
|
1.0
|
CG
|
B:GLU406
|
4.3
|
7.4
|
1.0
|
CZ
|
B:TYR472
|
4.3
|
12.0
|
1.0
|
OE1
|
B:GLU350
|
4.4
|
8.3
|
1.0
|
CA
|
B:GLU406
|
4.6
|
8.7
|
1.0
|
CB
|
B:GLU406
|
4.7
|
9.7
|
1.0
|
CD2
|
B:TYR472
|
4.7
|
14.0
|
1.0
|
O
|
B:HOH1258
|
4.9
|
10.0
|
1.0
|
OE2
|
B:GLU384
|
4.9
|
12.6
|
1.0
|
|
Zinc binding site 3 out
of 4 in 5lds
Go back to
Zinc Binding Sites List in 5lds
Zinc binding site 3 out
of 4 in the Structure of the Porcine Aminopeptidase N Ectodomain
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 3 of Structure of the Porcine Aminopeptidase N Ectodomain within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Zn1001
b:9.5
occ:1.00
|
O
|
C:ACT1011
|
1.9
|
12.2
|
1.0
|
OE1
|
C:GLU406
|
2.0
|
11.8
|
1.0
|
NE2
|
C:HIS383
|
2.0
|
7.3
|
1.0
|
NE2
|
C:HIS387
|
2.1
|
11.0
|
1.0
|
C
|
C:ACT1011
|
2.6
|
15.8
|
1.0
|
OXT
|
C:ACT1011
|
2.6
|
13.2
|
1.0
|
CD
|
C:GLU406
|
2.8
|
7.3
|
1.0
|
CE1
|
C:HIS383
|
3.0
|
12.8
|
1.0
|
CD2
|
C:HIS387
|
3.0
|
7.5
|
1.0
|
CD2
|
C:HIS383
|
3.0
|
14.4
|
1.0
|
OE2
|
C:GLU406
|
3.0
|
7.8
|
1.0
|
CE1
|
C:HIS387
|
3.0
|
7.5
|
1.0
|
O
|
C:HOH1192
|
3.6
|
5.5
|
1.0
|
CE2
|
C:TYR472
|
3.9
|
10.5
|
1.0
|
OH
|
C:TYR472
|
4.0
|
11.3
|
1.0
|
CB
|
C:ALA409
|
4.0
|
7.6
|
1.0
|
CH3
|
C:ACT1011
|
4.0
|
19.5
|
1.0
|
ND1
|
C:HIS383
|
4.1
|
12.8
|
1.0
|
CG
|
C:HIS383
|
4.1
|
8.0
|
1.0
|
CG
|
C:HIS387
|
4.2
|
7.6
|
1.0
|
ND1
|
C:HIS387
|
4.2
|
7.7
|
1.0
|
CZ
|
C:TYR472
|
4.3
|
12.7
|
1.0
|
CG
|
C:GLU406
|
4.3
|
9.6
|
1.0
|
OE1
|
C:GLU350
|
4.4
|
7.3
|
1.0
|
CA
|
C:GLU406
|
4.7
|
14.0
|
1.0
|
CB
|
C:GLU406
|
4.7
|
15.6
|
1.0
|
CD2
|
C:TYR472
|
4.8
|
7.1
|
1.0
|
OE2
|
C:GLU384
|
4.8
|
13.3
|
1.0
|
OE2
|
C:GLU350
|
4.9
|
9.3
|
1.0
|
CD
|
C:GLU350
|
5.0
|
7.5
|
1.0
|
O
|
C:HOH1314
|
5.0
|
7.0
|
1.0
|
|
Zinc binding site 4 out
of 4 in 5lds
Go back to
Zinc Binding Sites List in 5lds
Zinc binding site 4 out
of 4 in the Structure of the Porcine Aminopeptidase N Ectodomain
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 4 of Structure of the Porcine Aminopeptidase N Ectodomain within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Zn1001
b:6.9
occ:1.00
|
OXT
|
D:ACT1020
|
1.9
|
6.2
|
1.0
|
OE1
|
D:GLU406
|
1.9
|
7.4
|
1.0
|
NE2
|
D:HIS383
|
2.0
|
3.7
|
1.0
|
NE2
|
D:HIS387
|
2.1
|
4.9
|
1.0
|
C
|
D:ACT1020
|
2.6
|
13.9
|
1.0
|
O
|
D:ACT1020
|
2.6
|
10.6
|
1.0
|
CD
|
D:GLU406
|
2.9
|
9.8
|
1.0
|
CE1
|
D:HIS383
|
3.0
|
4.2
|
1.0
|
CD2
|
D:HIS387
|
3.0
|
4.8
|
1.0
|
CD2
|
D:HIS383
|
3.1
|
3.7
|
1.0
|
CE1
|
D:HIS387
|
3.1
|
6.2
|
1.0
|
OE2
|
D:GLU406
|
3.1
|
3.8
|
1.0
|
O
|
D:HOH1251
|
3.4
|
4.5
|
1.0
|
CE2
|
D:TYR472
|
3.8
|
12.1
|
1.0
|
OH
|
D:TYR472
|
4.0
|
5.1
|
1.0
|
CH3
|
D:ACT1020
|
4.0
|
14.9
|
1.0
|
ND1
|
D:HIS383
|
4.1
|
3.8
|
1.0
|
CG
|
D:HIS387
|
4.2
|
3.8
|
1.0
|
CG
|
D:HIS383
|
4.2
|
4.1
|
1.0
|
CB
|
D:ALA409
|
4.2
|
3.7
|
1.0
|
ND1
|
D:HIS387
|
4.2
|
6.7
|
1.0
|
CG
|
D:GLU406
|
4.3
|
6.5
|
1.0
|
CZ
|
D:TYR472
|
4.3
|
10.8
|
1.0
|
OE1
|
D:GLU350
|
4.4
|
6.3
|
1.0
|
CA
|
D:GLU406
|
4.6
|
5.9
|
1.0
|
CB
|
D:GLU406
|
4.7
|
9.0
|
1.0
|
CD2
|
D:TYR472
|
4.8
|
10.2
|
1.0
|
OE2
|
D:GLU384
|
4.9
|
10.4
|
1.0
|
O
|
D:HOH1220
|
4.9
|
6.7
|
1.0
|
CD
|
D:GLU350
|
5.0
|
3.8
|
1.0
|
|
Reference:
C.Santiago,
G.Mudgal,
J.Reguera,
R.Recacha,
S.Albrecht,
L.Enjuanes,
J.M.Casasnovas.
Allosteric Inhibition of Aminopeptidase N Functions Related to Tumor Growth and Virus Infection. Sci Rep V. 7 46045 2017.
ISSN: ESSN 2045-2322
PubMed: 28393915
DOI: 10.1038/SREP46045
Page generated: Sun Oct 27 20:58:22 2024
|