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Sodium 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:

Zinc (Zn) 1 atom

Sodium Binding Sites:

The binding sites of Sodium 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 Sodium atom.
In total only one binding site of Sodium was determined in the Carboxypeptidase A Liganded to An Organic Small-Molecule: Conformational Changes, PDB code: 3kgq:

Sodium binding site 1 out of 1 in 3kgq

Go back to Sodium Binding Sites List in 3kgq
Sodium 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 Sodium with other atoms in the Na 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:Na402

b:15.8
occ:1.00
 N A:LEU15 3.2 14.4 1.0
O A:HOH390 3.3 16.2 1.0
O A:HOH381 3.5 27.6 1.0
ND1 A:HIS120 3.5 17.9 1.0
CG A:HIS120 3.6 17.0 1.0
CB A:LEU15 3.8 15.3 1.0
CB A:THR14 3.8 14.6 1.0
CB A:HIS120 3.8 17.1 1.0
CA A:ALA117 3.8 13.1 1.0
CA A:THR14 3.9 14.7 1.0
C A:THR14 4.1 14.6 1.0
CA A:LEU15 4.1 15.2 1.0
CE1 A:HIS120 4.1 17.3 1.0
CD2 A:HIS120 4.3 18.1 1.0
O A:PHE116 4.4 12.7 1.0
CB A:ALA117 4.4 13.2 1.0
O A:ALA117 4.5 13.2 1.0
N A:ALA117 4.5 12.8 1.0
NE2 A:HIS120 4.5 17.2 1.0
CG2 A:THR14 4.6 15.7 1.0
C A:ALA117 4.7 13.3 1.0
C A:PHE116 4.7 12.7 1.0
OG1 A:THR14 4.8 15.2 1.0
CD2 A:PHE116 4.9 13.3 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: Tue Dec 15 06:16:15 2020

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