Zinc in PDB 3cia: Crystal Structure of Cold-Aminopeptidase From Colwellia Psychrerythraea
Protein crystallography data
The structure of Crystal Structure of Cold-Aminopeptidase From Colwellia Psychrerythraea, PDB code: 3cia
was solved by
C.Bauvois,
L.Jacquamet,
F.Borel,
J.-L.Ferrer,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
46.68 /
2.70
|
Space group
|
P 1
|
Cell size a, b, c (Å), α, β, γ (°)
|
81.370,
87.100,
116.360,
88.83,
70.68,
88.43
|
R / Rfree (%)
|
24.9 /
27
|
Zinc Binding Sites:
The binding sites of Zinc atom in the Crystal Structure of Cold-Aminopeptidase From Colwellia Psychrerythraea
(pdb code 3cia). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the
Crystal Structure of Cold-Aminopeptidase From Colwellia Psychrerythraea, PDB code: 3cia:
Jump to Zinc binding site number:
1;
2;
3;
4;
Zinc binding site 1 out
of 4 in 3cia
Go back to
Zinc Binding Sites List in 3cia
Zinc binding site 1 out
of 4 in the Crystal Structure of Cold-Aminopeptidase From Colwellia Psychrerythraea
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 1 of Crystal Structure of Cold-Aminopeptidase From Colwellia Psychrerythraea within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn701
b:9.8
occ:0.30
|
NE2
|
A:HIS328
|
2.7
|
8.8
|
1.0
|
OE2
|
A:GLU347
|
2.8
|
32.7
|
1.0
|
NE2
|
A:HIS324
|
3.0
|
20.0
|
1.0
|
CD2
|
A:HIS328
|
3.5
|
7.9
|
1.0
|
CE1
|
A:HIS328
|
3.6
|
8.5
|
1.0
|
OH
|
A:TYR410
|
3.7
|
20.8
|
1.0
|
CD2
|
A:HIS324
|
3.8
|
20.8
|
1.0
|
CE1
|
A:HIS324
|
3.9
|
19.8
|
1.0
|
CD
|
A:GLU347
|
3.9
|
30.0
|
1.0
|
OE1
|
A:GLU300
|
4.0
|
19.8
|
1.0
|
CE2
|
A:TYR410
|
4.0
|
23.2
|
1.0
|
OE1
|
A:GLU325
|
4.1
|
22.9
|
1.0
|
OE1
|
A:GLU347
|
4.2
|
33.9
|
1.0
|
CZ
|
A:TYR410
|
4.4
|
22.7
|
1.0
|
O
|
A:HOH765
|
4.4
|
6.9
|
1.0
|
CD
|
A:GLU300
|
4.7
|
19.1
|
1.0
|
CG
|
A:HIS328
|
4.7
|
8.9
|
1.0
|
ND1
|
A:HIS328
|
4.7
|
7.1
|
1.0
|
O
|
A:GLY298
|
4.8
|
25.8
|
1.0
|
OE2
|
A:GLU300
|
4.8
|
18.9
|
1.0
|
CG
|
A:HIS324
|
4.9
|
20.3
|
1.0
|
ND1
|
A:HIS324
|
4.9
|
18.9
|
1.0
|
|
Zinc binding site 2 out
of 4 in 3cia
Go back to
Zinc Binding Sites List in 3cia
Zinc binding site 2 out
of 4 in the Crystal Structure of Cold-Aminopeptidase From Colwellia Psychrerythraea
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 2 of Crystal Structure of Cold-Aminopeptidase From Colwellia Psychrerythraea within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Zn701
b:24.2
occ:0.30
|
NE2
|
B:HIS328
|
2.6
|
20.1
|
1.0
|
OE2
|
B:GLU347
|
2.7
|
26.1
|
1.0
|
NE2
|
B:HIS324
|
3.1
|
17.5
|
1.0
|
CE1
|
B:HIS328
|
3.5
|
21.1
|
1.0
|
CD2
|
B:HIS328
|
3.6
|
19.7
|
1.0
|
OH
|
B:TYR410
|
3.7
|
12.1
|
1.0
|
CD
|
B:GLU347
|
3.8
|
25.3
|
1.0
|
OE1
|
B:GLU300
|
3.9
|
29.0
|
1.0
|
CD2
|
B:HIS324
|
3.9
|
18.1
|
1.0
|
CE1
|
B:HIS324
|
4.0
|
15.8
|
1.0
|
CE2
|
B:TYR410
|
4.0
|
16.7
|
1.0
|
OE1
|
B:GLU325
|
4.1
|
20.8
|
1.0
|
OE1
|
B:GLU347
|
4.2
|
27.8
|
1.0
|
CZ
|
B:TYR410
|
4.3
|
14.8
|
1.0
|
CD
|
B:GLU300
|
4.6
|
28.2
|
1.0
|
ND1
|
B:HIS328
|
4.7
|
20.6
|
1.0
|
O
|
B:GLY298
|
4.7
|
24.1
|
1.0
|
CG
|
B:HIS328
|
4.8
|
19.3
|
1.0
|
OE2
|
B:GLU300
|
4.8
|
29.7
|
1.0
|
|
Zinc binding site 3 out
of 4 in 3cia
Go back to
Zinc Binding Sites List in 3cia
Zinc binding site 3 out
of 4 in the Crystal Structure of Cold-Aminopeptidase From Colwellia Psychrerythraea
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 3 of Crystal Structure of Cold-Aminopeptidase From Colwellia Psychrerythraea within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Zn701
b:15.4
occ:0.30
|
NE2
|
C:HIS328
|
2.7
|
26.1
|
1.0
|
OE2
|
C:GLU347
|
2.7
|
34.8
|
1.0
|
NE2
|
C:HIS324
|
3.0
|
19.9
|
1.0
|
CD2
|
C:HIS328
|
3.6
|
23.7
|
1.0
|
CE1
|
C:HIS328
|
3.6
|
24.4
|
1.0
|
OH
|
C:TYR410
|
3.7
|
16.4
|
1.0
|
CD
|
C:GLU347
|
3.8
|
32.1
|
1.0
|
CD2
|
C:HIS324
|
3.9
|
20.9
|
1.0
|
OE1
|
C:GLU300
|
3.9
|
23.0
|
1.0
|
CE1
|
C:HIS324
|
4.0
|
19.5
|
1.0
|
CE2
|
C:TYR410
|
4.0
|
15.5
|
1.0
|
OE1
|
C:GLU325
|
4.1
|
21.2
|
1.0
|
OE1
|
C:GLU347
|
4.2
|
34.7
|
1.0
|
CZ
|
C:TYR410
|
4.3
|
16.2
|
1.0
|
CD
|
C:GLU300
|
4.6
|
20.2
|
1.0
|
O
|
C:GLY298
|
4.7
|
29.3
|
1.0
|
ND1
|
C:HIS328
|
4.8
|
23.5
|
1.0
|
CG
|
C:HIS328
|
4.8
|
23.8
|
1.0
|
OE2
|
C:GLU300
|
4.8
|
20.8
|
1.0
|
CG
|
C:HIS324
|
5.0
|
21.7
|
1.0
|
|
Zinc binding site 4 out
of 4 in 3cia
Go back to
Zinc Binding Sites List in 3cia
Zinc binding site 4 out
of 4 in the Crystal Structure of Cold-Aminopeptidase From Colwellia Psychrerythraea
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 4 of Crystal Structure of Cold-Aminopeptidase From Colwellia Psychrerythraea within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Zn701
b:28.3
occ:0.40
|
NE2
|
D:HIS328
|
2.6
|
17.8
|
1.0
|
OE2
|
D:GLU347
|
2.7
|
33.8
|
1.0
|
NE2
|
D:HIS324
|
3.1
|
24.9
|
1.0
|
O
|
D:HOH911
|
3.1
|
59.4
|
1.0
|
CD2
|
D:HIS328
|
3.5
|
17.9
|
1.0
|
CE1
|
D:HIS328
|
3.6
|
16.6
|
1.0
|
OH
|
D:TYR410
|
3.7
|
22.0
|
1.0
|
CD
|
D:GLU347
|
3.8
|
31.5
|
1.0
|
CD2
|
D:HIS324
|
3.9
|
25.8
|
1.0
|
CE1
|
D:HIS324
|
4.0
|
24.7
|
1.0
|
OE1
|
D:GLU300
|
4.0
|
20.6
|
1.0
|
CE2
|
D:TYR410
|
4.0
|
22.8
|
1.0
|
OE1
|
D:GLU325
|
4.1
|
24.0
|
1.0
|
OE1
|
D:GLU347
|
4.2
|
32.3
|
1.0
|
CZ
|
D:TYR410
|
4.3
|
22.6
|
1.0
|
O
|
D:HOH790
|
4.4
|
33.2
|
1.0
|
CD
|
D:GLU300
|
4.6
|
20.6
|
1.0
|
ND1
|
D:HIS328
|
4.7
|
15.7
|
1.0
|
CG
|
D:HIS328
|
4.7
|
16.9
|
1.0
|
O
|
D:HOH970
|
4.7
|
41.4
|
1.0
|
OE2
|
D:GLU300
|
4.7
|
20.5
|
1.0
|
O
|
D:GLY298
|
4.8
|
28.1
|
1.0
|
CG
|
D:HIS324
|
5.0
|
25.5
|
1.0
|
|
Reference:
C.Bauvois,
L.Jacquamet,
A.L.Huston,
F.Borel,
G.Feller,
J.L.Ferrer.
Crystal Structure of the Cold-Active Aminopeptidase From Colwellia Psychrerythraea, A Close Structural Homologue of the Human Bifunctional Leukotriene A4 Hydrolase. J.Biol.Chem. V. 283 23315 2008.
ISSN: ISSN 0021-9258
PubMed: 18539590
DOI: 10.1074/JBC.M802158200
Page generated: Thu Oct 24 11:49:15 2024
|