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Zinc in PDB 2gkl: Crystal Structure of the Zinc Carbapenemase Cpha in Complex with the Inhibitor Pyridine-2,4-Dicarboxylate

Enzymatic activity of Crystal Structure of the Zinc Carbapenemase Cpha in Complex with the Inhibitor Pyridine-2,4-Dicarboxylate

All present enzymatic activity of Crystal Structure of the Zinc Carbapenemase Cpha in Complex with the Inhibitor Pyridine-2,4-Dicarboxylate:
3.5.2.6;

Protein crystallography data

The structure of Crystal Structure of the Zinc Carbapenemase Cpha in Complex with the Inhibitor Pyridine-2,4-Dicarboxylate, PDB code: 2gkl 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) 21.90 / 1.86
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 42.638, 101.211, 117.121, 90.00, 90.00, 90.00
R / Rfree (%) 15.9 / 19.6

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of the Zinc Carbapenemase Cpha in Complex with the Inhibitor Pyridine-2,4-Dicarboxylate (pdb code 2gkl). 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 Pyridine-2,4-Dicarboxylate, PDB code: 2gkl:

Zinc binding site 1 out of 1 in 2gkl

Go back to Zinc Binding Sites List in 2gkl
Zinc binding site 1 out of 1 in the Crystal Structure of the Zinc Carbapenemase Cpha in Complex with the Inhibitor Pyridine-2,4-Dicarboxylate


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 Pyridine-2,4-Dicarboxylate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn401

b:19.8
occ:1.00
 OD2 A:ASP120 2.1 17.0 1.0
NE2 A:HIS263 2.2 13.9 1.0
N1 A:PD22 2.2 19.5 1.0
O22 A:PD22 2.3 17.4 1.0
SG A:CYS221 2.3 14.7 1.0
C2 A:PD22 3.0 19.2 1.0
C21 A:PD22 3.0 21.0 1.0
CE1 A:HIS263 3.1 14.8 1.0
C6 A:PD22 3.1 20.4 1.0
CG A:ASP120 3.2 14.2 1.0
CD2 A:HIS263 3.2 15.4 1.0
CB A:CYS221 3.4 15.5 1.0
OD1 A:ASP120 3.6 15.8 1.0
O A:HOH405 3.9 31.4 1.0
NH2 A:ARG121 4.0 15.7 1.0
CA A:CYS221 4.1 14.7 1.0
ND1 A:HIS263 4.2 13.0 1.0
O21 A:PD22 4.2 21.2 1.0
NE2 A:HIS196 4.3 16.2 1.0
CG A:HIS263 4.3 12.9 1.0
CE1 A:HIS196 4.3 17.1 1.0
C3 A:PD22 4.3 21.1 1.0
O A:HOH408 4.4 22.3 1.0
C5 A:PD22 4.4 20.8 1.0
CB A:ASP120 4.4 12.6 1.0
NE A:ARG121 4.6 12.1 1.0
CZ A:ARG121 4.7 13.1 1.0
C4 A:PD22 4.9 22.0 1.0
N A:CYS221 5.0 14.1 1.0

Reference:

L.E.Horsfall, G.Garau, B.M.R.Lienard, O.Dideberg, C.J.Schofield, J.M.Frere, M.Galleni. Competitive Inhibitors of the Cpha Metallo-{Beta}-Lactamase From Aeromonas Hydrophila Antimicrob.Agents Chemother. V. 51 2136 2007.
ISSN: ISSN 0066-4804
PubMed: 17307979
DOI: 10.1128/AAC.00866-06
Page generated: Thu Oct 17 00:19:39 2024

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