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Zinc in PDB 2hpo: Structure of Aminopeptidase N From E. Coli Suggests A Compartmentalized, Gated Active Site

Enzymatic activity of Structure of Aminopeptidase N From E. Coli Suggests A Compartmentalized, Gated Active Site

All present enzymatic activity of Structure of Aminopeptidase N From E. Coli Suggests A Compartmentalized, Gated Active Site:
3.4.11.2;

Protein crystallography data

The structure of Structure of Aminopeptidase N From E. Coli Suggests A Compartmentalized, Gated Active Site, PDB code: 2hpo was solved by A.Addlagatta, B.W.Matthews, L.Gay, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 19.94 / 1.65
Space group P 31 2 1
Cell size a, b, c (Å), α, β, γ (°) 120.438, 120.438, 170.561, 90.00, 90.00, 120.00
R / Rfree (%) 15.7 / 18.1

Zinc Binding Sites:

The binding sites of Zinc atom in the Structure of Aminopeptidase N From E. Coli Suggests A Compartmentalized, Gated Active Site (pdb code 2hpo). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the Structure of Aminopeptidase N From E. Coli Suggests A Compartmentalized, Gated Active Site, PDB code: 2hpo:

Zinc binding site 1 out of 1 in 2hpo

Go back to Zinc Binding Sites List in 2hpo
Zinc binding site 1 out of 1 in the Structure of Aminopeptidase N From E. Coli Suggests A Compartmentalized, Gated Active Site


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structure of Aminopeptidase N From E. Coli Suggests A Compartmentalized, Gated Active Site within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn1250

b:8.8
occ:1.00
 OE1 A:GLU320 2.0 7.2 1.0
NE2 A:HIS297 2.0 7.8 1.0
NE2 A:HIS301 2.0 8.8 1.0
O A:HOH1272 2.1 13.4 1.0
CD A:GLU320 2.7 6.4 1.0
OE2 A:GLU320 2.7 8.7 1.0
CE1 A:HIS301 3.0 6.5 1.0
CE1 A:HIS297 3.0 9.5 1.0
CD2 A:HIS297 3.0 8.9 1.0
CD2 A:HIS301 3.0 7.7 1.0
O A:HOH1961 3.8 25.5 1.0
O A:HOH1298 3.9 12.8 1.0
CE2 A:TYR381 3.9 8.1 1.0
OH A:TYR381 4.0 9.7 1.0
ND1 A:HIS301 4.1 7.0 1.0
ND1 A:HIS297 4.1 7.9 1.0
CG A:HIS297 4.2 7.3 1.0
CG A:HIS301 4.2 6.9 1.0
CG A:GLU320 4.2 7.2 1.0
CZ A:TYR381 4.3 9.0 1.0
CG2 A:THR323 4.5 7.0 1.0
OE1 A:GLU264 4.6 6.9 1.0
OE1 A:GLU298 4.6 12.3 1.0
CB A:THR323 4.6 6.9 1.0
CA A:GLU320 4.7 7.4 1.0
CB A:GLU320 4.7 7.0 1.0
NZ A:LYS319 4.9 6.5 1.0
CD2 A:TYR381 4.9 7.6 1.0
OE2 A:GLU264 4.9 8.8 1.0
OE2 A:GLU298 4.9 11.9 1.0
CD A:GLU264 5.0 7.6 1.0

Reference:

A.Addlagatta, L.Gay, B.W.Matthews. Structure of Aminopeptidase N From Escherichia Coli Suggests A Compartmentalized, Gated Active Site. Proc.Natl.Acad.Sci.Usa V. 103 13339 2006.
ISSN: ISSN 0027-8424
PubMed: 16938892
DOI: 10.1073/PNAS.0606167103
Page generated: Thu Oct 17 00:40:55 2024

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