Atomistry » Zinc » PDB 4ntn-4o6o » 4nz8
Atomistry »
  Zinc »
    PDB 4ntn-4o6o »
      4nz8 »

Zinc in PDB 4nz8: Crystal Structure of Porcine Aminopeptidase-N Complexed with Cleaved Poly-Alanine

Enzymatic activity of Crystal Structure of Porcine Aminopeptidase-N Complexed with Cleaved Poly-Alanine

All present enzymatic activity of Crystal Structure of Porcine Aminopeptidase-N Complexed with Cleaved Poly-Alanine:
3.4.11.2;

Protein crystallography data

The structure of Crystal Structure of Porcine Aminopeptidase-N Complexed with Cleaved Poly-Alanine, PDB code: 4nz8 was solved by L.Chen, Y.L.Lin, G.Peng, F.Li, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 50.00 / 2.00
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 261.977, 62.884, 81.862, 90.00, 100.39, 90.00
R / Rfree (%) 15 / 20.8

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of Porcine Aminopeptidase-N Complexed with Cleaved Poly-Alanine (pdb code 4nz8). 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 Porcine Aminopeptidase-N Complexed with Cleaved Poly-Alanine, PDB code: 4nz8:

Zinc binding site 1 out of 1 in 4nz8

Go back to Zinc Binding Sites List in 4nz8
Zinc binding site 1 out of 1 in the Crystal Structure of Porcine Aminopeptidase-N Complexed with Cleaved Poly-Alanine


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 Porcine Aminopeptidase-N Complexed with Cleaved Poly-Alanine within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn1016

b:43.0
occ:1.00
OE1 A:GLU406 2.0 33.8 1.0
NE2 A:HIS387 2.1 31.3 1.0
NE2 A:HIS383 2.1 34.2 1.0
O A:HOH1716 2.1 44.3 1.0
CD A:GLU406 2.8 31.1 1.0
OE2 A:GLU406 2.9 34.0 1.0
CD2 A:HIS383 3.0 31.9 1.0
CD2 A:HIS387 3.1 27.8 1.0
CE1 A:HIS387 3.1 30.0 1.0
CE1 A:HIS383 3.1 31.9 1.0
O B:ALA1 3.7 49.1 1.0
C B:ALA1 4.1 57.0 1.0
CB A:ALA409 4.1 32.5 1.0
CB C:ALA3 4.2 64.9 1.0
OE1 A:GLU350 4.2 31.7 1.0
CG A:GLU406 4.2 29.4 1.0
CG A:HIS383 4.2 33.2 1.0
CG A:HIS387 4.2 30.8 1.0
ND1 A:HIS383 4.2 33.1 1.0
ND1 A:HIS387 4.2 31.6 1.0
OE1 A:GLU384 4.3 36.9 1.0
N B:ALA1 4.4 40.0 1.0
CE2 A:TYR472 4.5 32.0 1.0
CA A:GLU406 4.6 30.9 1.0
CD A:GLU350 4.6 30.5 1.0
CA B:ALA1 4.7 49.9 1.0
CB A:GLU406 4.7 28.6 1.0
OE2 A:GLU384 4.7 39.0 1.0
OE2 A:GLU350 4.8 32.0 1.0
OH A:TYR472 4.8 33.4 1.0
CD A:GLU384 4.9 37.4 1.0

Reference:

L.Chen, Y.L.Lin, G.Peng, F.Li. Structural Basis For Multifunctional Roles of Mammalian Aminopeptidase N. Proc.Natl.Acad.Sci.Usa V. 109 17966 2012.
ISSN: ISSN 0027-8424
PubMed: 23071329
DOI: 10.1073/PNAS.1210123109
Page generated: Wed Dec 16 05:38:03 2020

Last articles

Zn in 8WB0
Zn in 8WAX
Zn in 8WAU
Zn in 8WAZ
Zn in 8WAY
Zn in 8WAV
Zn in 8WAW
Zn in 8WAT
Zn in 8W7M
Zn in 8WD3
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy