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Zinc in PDB 3kgq: Carboxypeptidase A Liganded to An Organic Small-Molecule: Conformational Changes

Enzymatic activity of Carboxypeptidase A Liganded to An Organic Small-Molecule: Conformational Changes

All present enzymatic activity of Carboxypeptidase A Liganded to An Organic Small-Molecule: Conformational Changes:
3.4.17.1;

Protein crystallography data

The structure of Carboxypeptidase A Liganded to An Organic Small-Molecule: Conformational Changes, PDB code: 3kgq was solved by D.Fernandez, E.Boix, I.Pallares, F.X.Aviles, J.Vendrell, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.24 / 1.70
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 40.604, 57.006, 60.604, 90.00, 102.04, 90.00
R / Rfree (%) 18 / 20.4

Other elements in 3kgq:

The structure of Carboxypeptidase A Liganded to An Organic Small-Molecule: Conformational Changes also contains other interesting chemical elements:

Sodium (Na) 1 atom

Zinc Binding Sites:

The binding sites of Zinc atom in the Carboxypeptidase A Liganded to An Organic Small-Molecule: Conformational Changes (pdb code 3kgq). 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 Carboxypeptidase A Liganded to An Organic Small-Molecule: Conformational Changes, PDB code: 3kgq:

Zinc binding site 1 out of 1 in 3kgq

Go back to Zinc Binding Sites List in 3kgq
Zinc binding site 1 out of 1 in the Carboxypeptidase A Liganded to An Organic Small-Molecule: Conformational Changes


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Carboxypeptidase A Liganded to An Organic Small-Molecule: Conformational Changes within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn401

b:13.6
occ:1.00
 OE2 A:GLU72 2.1 13.8 1.0
O2 A:CIT310 2.1 20.3 1.0
ND1 A:HIS196 2.1 11.2 1.0
ND1 A:HIS69 2.1 11.8 1.0
O1 A:CIT310 2.5 20.8 1.0
OE1 A:GLU72 2.6 12.3 1.0
C1 A:CIT310 2.6 18.9 1.0
CD A:GLU72 2.7 12.6 1.0
CE1 A:HIS196 3.0 11.6 1.0
CE1 A:HIS69 3.0 12.6 1.0
CG A:HIS69 3.1 12.4 1.0
CG A:HIS196 3.1 11.5 1.0
CB A:HIS69 3.5 11.9 1.0
CB A:HIS196 3.5 11.7 1.0
O7 A:CIT310 3.9 20.8 1.0
NH1 A:ARG127 4.1 17.1 1.0
C2 A:CIT310 4.1 20.0 1.0
O A:HOH349 4.1 15.2 1.0
O A:SER197 4.1 12.3 1.0
NE2 A:HIS196 4.1 11.6 1.0
CG A:GLU72 4.1 12.3 1.0
NE2 A:HIS69 4.2 13.4 1.0
CD2 A:HIS69 4.2 12.8 1.0
CD2 A:HIS196 4.2 11.2 1.0
O A:HOH330 4.3 13.4 1.0
C3 A:CIT310 4.4 19.7 1.0
O6 A:CIT310 4.4 17.3 1.0
CA A:HIS196 4.4 11.8 1.0
C6 A:CIT310 4.4 18.9 1.0
N A:SER197 4.6 12.3 1.0
CA A:HIS69 4.8 11.7 1.0
CZ A:ARG127 4.9 16.9 1.0
OE1 A:GLU270 4.9 17.0 1.0
N A:HIS69 5.0 11.6 1.0

Reference:

D.Fernandez, E.Boix, I.Pallares, F.X.Aviles, J.Vendrell. Structural and Functional Analysis of the Complex Between Citrate and the Zinc Peptidase Carboxypeptidase A Enzyme Res V.2011 28676 2011.
ISSN: ISSN 2090-0406
PubMed: 21804935
DOI: 10.4061/2011/128676
Page generated: Wed Dec 16 04:30:06 2020

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