Atomistry » Zinc » PDB 2q1z-2ql1 » 2qds
Atomistry »
  Zinc »
    PDB 2q1z-2ql1 »
      2qds »

Zinc in PDB 2qds: Crystal Structure of the Zinc Carbapenemase Cpha in Complex with the Inhibitor D-Captopril

Enzymatic activity of Crystal Structure of the Zinc Carbapenemase Cpha in Complex with the Inhibitor D-Captopril

All present enzymatic activity of Crystal Structure of the Zinc Carbapenemase Cpha in Complex with the Inhibitor D-Captopril:
3.5.2.6;

Protein crystallography data

The structure of Crystal Structure of the Zinc Carbapenemase Cpha in Complex with the Inhibitor D-Captopril, PDB code: 2qds was solved by G.Garau, O.Dideberg, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 50.00 / 1.66
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 43.001, 100.990, 116.819, 90.00, 90.00, 90.00
R / Rfree (%) 14.8 / 17

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of the Zinc Carbapenemase Cpha in Complex with the Inhibitor D-Captopril (pdb code 2qds). 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 the Zinc Carbapenemase Cpha in Complex with the Inhibitor D-Captopril, PDB code: 2qds:

Zinc binding site 1 out of 1 in 2qds

Go back to Zinc Binding Sites List in 2qds
Zinc binding site 1 out of 1 in the Crystal Structure of the Zinc Carbapenemase Cpha in Complex with the Inhibitor D-Captopril


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 the Zinc Carbapenemase Cpha in Complex with the Inhibitor D-Captopril within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn401

b:14.6
occ:1.00
 OD2 A:ASP120 2.0 12.4 1.0
O2 A:MCO501 2.0 24.4 1.0
NE2 A:HIS263 2.1 12.6 1.0
SG A:CYS221 2.3 13.5 1.0
CG A:ASP120 3.0 12.0 1.0
CE1 A:HIS263 3.0 11.7 1.0
C9 A:MCO501 3.1 30.2 1.0
CD2 A:HIS263 3.2 12.6 1.0
OD1 A:ASP120 3.3 11.8 1.0
CB A:CYS221 3.4 12.8 1.0
C8 A:MCO501 3.5 30.7 1.0
O A:HOH608 3.8 23.6 1.0
NH2 A:ARG121 3.9 12.0 1.0
C7 A:MCO501 4.0 31.1 1.0
ND1 A:HIS263 4.2 11.2 1.0
O3 A:MCO501 4.2 29.0 1.0
CA A:CYS221 4.3 12.7 1.0
CG A:HIS263 4.3 11.6 1.0
CB A:ASP120 4.3 9.5 1.0
O A:HOH609 4.4 52.0 1.0
CZ A:ARG121 4.4 9.8 1.0
CE1 A:HIS196 4.4 15.9 1.0
NE A:ARG121 4.4 9.0 1.0
NE2 A:HIS196 4.6 16.0 1.0
N A:MCO501 4.9 31.4 1.0
O1 A:MCO501 4.9 32.3 1.0
N A:CYS221 4.9 12.5 1.0

Reference:

B.M.Lienard, G.Garau, L.Horsfall, A.I.Karsisiotis, C.Damblon, P.Lassaux, C.Papamicael, G.C.Roberts, M.Galleni, O.Dideberg, J.M.Frere, C.J.Schofield. Structural Basis For the Broad-Spectrum Inhibition of Metallo-Beta-Lactamases By Thiols. Org.Biomol.Chem. V. 6 2282 2008.
ISSN: ISSN 1477-0520
PubMed: 18563261
DOI: 10.1039/B802311E
Page generated: Thu Oct 17 03:23:50 2024

Last articles

Zn in 9JYW
Zn in 9IR4
Zn in 9IR3
Zn in 9GMX
Zn in 9GMW
Zn in 9JEJ
Zn in 9ERF
Zn in 9ERE
Zn in 9EGV
Zn in 9EGW
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy