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Zinc in PDB 1x8g: Crystal Structure of the Mono-Zinc Carbapenemase Cpha From Aeromonas Hydrophyla

Enzymatic activity of Crystal Structure of the Mono-Zinc Carbapenemase Cpha From Aeromonas Hydrophyla

All present enzymatic activity of Crystal Structure of the Mono-Zinc Carbapenemase Cpha From Aeromonas Hydrophyla:
3.5.2.6;

Protein crystallography data

The structure of Crystal Structure of the Mono-Zinc Carbapenemase Cpha From Aeromonas Hydrophyla, PDB code: 1x8g 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) 25.00 / 1.70
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 42.628, 101.205, 118.239, 90.00, 90.00, 90.00
R / Rfree (%) 18.3 / 20.1

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of the Mono-Zinc Carbapenemase Cpha From Aeromonas Hydrophyla (pdb code 1x8g). 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 Mono-Zinc Carbapenemase Cpha From Aeromonas Hydrophyla, PDB code: 1x8g:

Zinc binding site 1 out of 1 in 1x8g

Go back to Zinc Binding Sites List in 1x8g
Zinc binding site 1 out of 1 in the Crystal Structure of the Mono-Zinc Carbapenemase Cpha From Aeromonas Hydrophyla


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 Mono-Zinc Carbapenemase Cpha From Aeromonas Hydrophyla within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn401

b:13.9
occ:1.00
OD2 A:ASP120 2.0 17.4 1.0
NE2 A:HIS263 2.1 12.0 1.0
O1 A:CO32 2.1 19.9 1.0
SG A:CYS221 2.2 12.3 1.0
C A:CO32 2.9 24.6 1.0
CD2 A:HIS263 3.0 12.5 1.0
CG A:ASP120 3.0 15.6 1.0
O2 A:CO32 3.1 24.3 1.0
CE1 A:HIS263 3.1 13.3 1.0
CB A:CYS221 3.2 14.8 1.0
OD1 A:ASP120 3.3 14.8 1.0
NH2 A:ARG121 3.9 13.8 1.0
O A:HOH403 4.0 29.9 1.0
CA A:CYS221 4.1 13.8 1.0
O3 A:CO32 4.1 29.2 1.0
CG A:HIS263 4.2 13.0 1.0
ND1 A:HIS263 4.2 13.7 1.0
CB A:ASP120 4.3 12.6 1.0
CZ A:ARG121 4.4 11.4 1.0
NE A:ARG121 4.4 11.8 1.0
NE2 A:HIS196 4.6 16.3 1.0
CE1 A:HIS196 4.6 15.6 1.0
N A:CYS221 4.8 13.8 1.0
O A:HOH406 4.8 27.7 1.0

Reference:

G.Garau, C.Bebrone, C.Anne, M.Galleni, J.M.Frere, O.Dideberg. A Metallo-Beta-Lactamase Enzyme in Action: Crystal Structures of the Monozinc Carbapenemase Cpha and Its Complex with Biapenem J.Mol.Biol. V. 345 785 2005.
ISSN: ISSN 0022-2836
PubMed: 15588826
DOI: 10.1016/J.JMB.2004.10.070
Page generated: Wed Dec 16 03:11:49 2020

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