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Zinc in PDB 4hom: Crystal Structure of Porcine Aminopeptidase-N Complexed with Substance P

Enzymatic activity of Crystal Structure of Porcine Aminopeptidase-N Complexed with Substance P

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

Protein crystallography data

The structure of Crystal Structure of Porcine Aminopeptidase-N Complexed with Substance P, PDB code: 4hom 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) 37.18 / 1.90
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 261.573, 62.598, 81.553, 90.00, 100.27, 90.00
R / Rfree (%) 14.7 / 20.1

Zinc Binding Sites:

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

Zinc binding site 1 out of 1 in 4hom

Go back to Zinc Binding Sites List in 4hom
Zinc binding site 1 out of 1 in the Crystal Structure of Porcine Aminopeptidase-N Complexed with Substance P


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 Substance P within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn1024

b:36.1
occ:1.00
OE2 A:GLU406 2.0 24.6 1.0
NE2 A:HIS383 2.1 24.9 1.0
NE2 A:HIS387 2.1 23.0 1.0
O A:HOH1506 2.1 35.4 1.0
CD A:GLU406 2.8 21.8 1.0
OE1 A:GLU406 2.9 24.8 1.0
CD2 A:HIS387 2.9 20.4 1.0
CD2 A:HIS383 2.9 22.7 1.0
CE1 A:HIS383 3.1 23.4 1.0
O B:ARG1 3.1 54.4 1.0
CE1 A:HIS387 3.2 21.6 1.0
C B:ARG1 3.9 58.9 1.0
OE2 A:GLU384 4.1 28.4 1.0
CG A:HIS383 4.1 23.6 1.0
OE1 A:GLU350 4.1 23.0 1.0
CG A:HIS387 4.1 22.4 1.0
CB A:ALA409 4.1 25.6 1.0
ND1 A:HIS383 4.2 23.2 1.0
ND1 A:HIS387 4.2 23.2 1.0
CG A:GLU406 4.2 20.0 1.0
N B:ARG1 4.3 42.9 1.0
CA B:PRO2 4.4 69.1 1.0
N B:PRO2 4.5 69.8 1.0
CE2 A:TYR472 4.5 23.3 1.0
CA A:GLU406 4.6 20.8 1.0
C B:PRO2 4.6 78.9 1.0
CA B:ARG1 4.6 66.2 1.0
CD A:GLU350 4.6 21.8 1.0
OE1 A:GLU384 4.6 28.4 1.0
CB A:GLU406 4.7 20.7 1.0
N B:LYS3 4.7 72.1 1.0
CD A:GLU384 4.7 27.0 1.0
OH A:TYR472 4.8 24.4 1.0
OE2 A:GLU350 4.9 22.4 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: Sun Oct 27 00:13:33 2024

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