Atomistry » Zinc » PDB 4fkh-4fvu » 4fkh
Atomistry »
  Zinc »
    PDB 4fkh-4fvu »
      4fkh »

Zinc in PDB 4fkh: Crystal Structure of Porcine Aminopeptidase-N Complexed with Alanine

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

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

Protein crystallography data

The structure of Crystal Structure of Porcine Aminopeptidase-N Complexed with Alanine, PDB code: 4fkh 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) 49.74 / 2.05
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 260.251, 62.892, 81.813, 90.00, 100.38, 90.00
R / Rfree (%) 12.9 / 18.9

Zinc Binding Sites:

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

Zinc binding site 1 out of 1 in 4fkh

Go back to Zinc Binding Sites List in 4fkh
Zinc binding site 1 out of 1 in the Crystal Structure of Porcine Aminopeptidase-N Complexed with 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 Alanine within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn1025

b:23.2
occ:1.00
OE2 A:GLU406 1.9 20.5 1.0
O A:HOH1524 2.0 22.4 1.0
NE2 A:HIS383 2.0 19.6 1.0
NE2 A:HIS387 2.1 17.8 1.0
CD A:GLU406 2.7 19.7 1.0
OE1 A:GLU406 2.8 20.9 1.0
CD2 A:HIS387 3.0 17.1 1.0
CD2 A:HIS383 3.0 20.1 1.0
CE1 A:HIS383 3.1 19.6 1.0
CE1 A:HIS387 3.2 19.2 1.0
O A:ALA1024 3.3 48.5 1.0
OE1 A:GLU350 4.0 18.8 1.0
CB A:ALA409 4.1 19.6 1.0
O A:HOH1498 4.1 41.3 1.0
C A:ALA1024 4.1 53.1 1.0
CG A:HIS383 4.1 19.3 1.0
CG A:GLU406 4.1 18.4 1.0
ND1 A:HIS383 4.1 21.5 1.0
CG A:HIS387 4.2 17.9 1.0
ND1 A:HIS387 4.2 19.6 1.0
OE2 A:GLU384 4.2 22.4 1.0
N A:ALA1024 4.3 30.4 1.0
CD A:GLU350 4.5 20.5 1.0
CA A:ALA1024 4.5 51.8 1.0
CE2 A:TYR472 4.6 19.5 1.0
CA A:GLU406 4.6 19.0 1.0
CB A:GLU406 4.7 18.8 1.0
OE2 A:GLU350 4.8 22.9 1.0
OH A:TYR472 4.8 24.4 1.0
O A:HOH1159 4.9 38.5 1.0
OE1 A:GLU384 5.0 25.3 1.0
CD A:GLU384 5.0 25.2 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: Sat Oct 26 22:49:37 2024

Last articles

Zn in 9J0N
Zn in 9J0O
Zn in 9J0P
Zn in 9FJX
Zn in 9EKB
Zn in 9C0F
Zn in 9CAH
Zn in 9CH0
Zn in 9CH3
Zn in 9CH1
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy