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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

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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

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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

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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

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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: Wed Dec 16 04:10:46 2020

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