Atomistry » Zinc » PDB 2hae-2hpt » 2hpt
Atomistry »
  Zinc »
    PDB 2hae-2hpt »
      2hpt »

Zinc in PDB 2hpt: Crystal Structure of E. Coli Pepn (Aminopeptidase N)in Complex with Bestatin

Enzymatic activity of Crystal Structure of E. Coli Pepn (Aminopeptidase N)in Complex with Bestatin

All present enzymatic activity of Crystal Structure of E. Coli Pepn (Aminopeptidase N)in Complex with Bestatin:
3.4.11.2;

Protein crystallography data

The structure of Crystal Structure of E. Coli Pepn (Aminopeptidase N)in Complex with Bestatin, PDB code: 2hpt 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) 49.94 / 2.30
Space group P 31 2 1
Cell size a, b, c (Å), α, β, γ (°) 120.670, 120.670, 170.840, 90.00, 90.00, 120.00
R / Rfree (%) 15.4 / 20.2

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of E. Coli Pepn (Aminopeptidase N)in Complex with Bestatin (pdb code 2hpt). 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 Crystal Structure of E. Coli Pepn (Aminopeptidase N)in Complex with Bestatin, PDB code: 2hpt:

Zinc binding site 1 out of 1 in 2hpt

Go back to Zinc Binding Sites List in 2hpt
Zinc binding site 1 out of 1 in the Crystal Structure of E. Coli Pepn (Aminopeptidase N)in Complex with Bestatin


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 E. Coli Pepn (Aminopeptidase N)in Complex with Bestatin within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn950

b:21.4
occ:1.00
O2 A:BES960 1.9 14.5 1.0
OE1 A:GLU320 2.1 14.4 1.0
NE2 A:HIS297 2.1 11.0 1.0
NE2 A:HIS301 2.1 7.3 1.0
O3 A:BES960 2.5 22.4 1.0
CD A:GLU320 2.9 14.3 1.0
C2 A:BES960 2.9 17.1 1.0
C3 A:BES960 2.9 18.1 1.0
OE2 A:GLU320 3.0 14.3 1.0
CD2 A:HIS297 3.0 7.7 1.0
CD2 A:HIS301 3.1 4.3 1.0
CE1 A:HIS297 3.1 9.1 1.0
CE1 A:HIS301 3.1 5.8 1.0
C1 A:BES960 3.6 16.6 1.0
N2 A:BES960 3.8 10.1 1.0
OE1 A:GLU298 3.9 11.6 1.0
OH A:TYR381 4.0 12.8 1.0
N1 A:BES960 4.2 18.0 1.0
CE2 A:TYR381 4.2 11.6 1.0
CG A:HIS297 4.2 11.1 1.0
ND1 A:HIS297 4.2 10.7 1.0
ND1 A:HIS301 4.2 8.3 1.0
CG A:HIS301 4.2 8.2 1.0
CG A:GLU320 4.3 11.6 1.0
CZ A:TYR381 4.5 11.8 1.0
OE2 A:GLU298 4.5 14.2 1.0
OE1 A:GLU264 4.5 12.2 1.0
CD A:GLU298 4.6 13.2 1.0
CG2 A:THR323 4.7 8.9 1.0
OE2 A:GLU264 4.8 8.9 1.0
CA A:GLU320 4.8 10.8 1.0
CB A:GLU320 4.8 10.3 1.0
CD A:GLU264 4.9 11.7 1.0
C15 A:BES960 4.9 17.2 1.0
CB A:THR323 4.9 11.1 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 00:41:03 2024

Last articles

Zn in 9JYW
Zn in 9IR4
Zn in 9IR3
Zn in 9GMX
Zn in 9GMW
Zn in 9JEJ
Zn in 9ERF
Zn in 9ERE
Zn in 9EGV
Zn in 9EGW
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy