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Zinc in PDB 4ou3: Crystal Structure of Porcine Aminopeptidase N Complexed with Cngrcg Tumor-Homing Peptide

Enzymatic activity of Crystal Structure of Porcine Aminopeptidase N Complexed with Cngrcg Tumor-Homing Peptide

All present enzymatic activity of Crystal Structure of Porcine Aminopeptidase N Complexed with Cngrcg Tumor-Homing Peptide:
3.4.11.2;

Protein crystallography data

The structure of Crystal Structure of Porcine Aminopeptidase N Complexed with Cngrcg Tumor-Homing Peptide, PDB code: 4ou3 was solved by C.Liu, Y.Yang, L.Chen, Y.-L.Lin, F.Li, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 50.00 / 1.95
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 260.323, 62.879, 82.023, 90.00, 100.59, 90.00
R / Rfree (%) 14 / 19

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of Porcine Aminopeptidase N Complexed with Cngrcg Tumor-Homing Peptide (pdb code 4ou3). 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 Cngrcg Tumor-Homing Peptide, PDB code: 4ou3:

Zinc binding site 1 out of 1 in 4ou3

Go back to Zinc Binding Sites List in 4ou3
Zinc binding site 1 out of 1 in the Crystal Structure of Porcine Aminopeptidase N Complexed with Cngrcg Tumor-Homing Peptide


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 Cngrcg Tumor-Homing Peptide within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn1001

b:30.2
occ:1.00
 OE2 A:GLU406 2.0 28.1 1.0
NE2 A:HIS387 2.0 23.2 1.0
NE2 A:HIS383 2.1 24.9 1.0
O A:HOH1232 2.2 28.6 1.0
CD A:GLU406 2.7 26.2 1.0
OE1 A:GLU406 2.7 28.1 1.0
CD2 A:HIS387 3.0 23.9 1.0
CD2 A:HIS383 3.0 25.1 1.0
CE1 A:HIS387 3.1 25.3 1.0
CE1 A:HIS383 3.2 26.1 1.0
O B:CYS1 3.3 30.9 1.0
C B:CYS1 3.9 35.0 1.0
OE1 A:GLU350 4.1 25.4 1.0
CB A:ALA409 4.1 26.0 1.0
N B:CYS1 4.1 26.6 1.0
CG A:HIS387 4.2 25.1 1.0
CG A:HIS383 4.2 25.9 1.0
ND1 A:HIS387 4.2 24.5 1.0
CG A:GLU406 4.2 24.2 1.0
ND1 A:HIS383 4.2 27.5 1.0
CB B:ASN2 4.3 39.2 1.0
OE1 A:GLU384 4.4 31.1 1.0
CE2 A:TYR472 4.5 26.9 1.0
N B:ASN2 4.5 36.6 1.0
CA B:CYS1 4.6 29.5 1.0
CD A:GLU350 4.6 24.4 1.0
CA A:GLU406 4.6 25.0 1.0
OE2 A:GLU384 4.7 29.7 1.0
CB A:GLU406 4.7 24.7 1.0
CA B:ASN2 4.8 38.5 1.0
OE2 A:GLU350 4.8 25.3 1.0
CD A:GLU384 4.9 28.5 1.0
CG B:ASN2 4.9 39.5 1.0
OH A:TYR472 4.9 28.4 1.0
O A:HOH1780 5.0 29.3 1.0

Reference:

C.Liu, Y.Yang, L.Chen, Y.-L.Lin, F.Li. A Unified Mechanism For Aminopeptidase N-Based Tumor Cell Motility and Tumor-Homing Therapy J.Biol.Chem. 2014.
ISSN: ESSN 1083-351X
DOI: 10.1074/JBC.M114.566802
Page generated: Sun Oct 27 04:00:07 2024

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