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Zinc in PDB 1x8i: Crystal Structure of the Zinc Carbapenemase Cpha in Complex with the Antibiotic Biapenem

Enzymatic activity of Crystal Structure of the Zinc Carbapenemase Cpha in Complex with the Antibiotic Biapenem

All present enzymatic activity of Crystal Structure of the Zinc Carbapenemase Cpha in Complex with the Antibiotic Biapenem:
3.5.2.6;

Protein crystallography data

The structure of Crystal Structure of the Zinc Carbapenemase Cpha in Complex with the Antibiotic Biapenem, PDB code: 1x8i 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) 26.50 / 1.90
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 42.836, 101.513, 117.364, 90.00, 90.00, 90.00
R / Rfree (%) 15.1 / 18.3

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of the Zinc Carbapenemase Cpha in Complex with the Antibiotic Biapenem (pdb code 1x8i). 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 Antibiotic Biapenem, PDB code: 1x8i:

Zinc binding site 1 out of 1 in 1x8i

Go back to Zinc Binding Sites List in 1x8i
Zinc binding site 1 out of 1 in the Crystal Structure of the Zinc Carbapenemase Cpha in Complex with the Antibiotic Biapenem


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 Antibiotic Biapenem within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn401

b:17.8
occ:1.00
 OD2 A:ASP120 2.0 12.9 1.0
NE2 A:HIS263 2.1 18.7 1.0
N4 A:BMH2 2.2 18.1 1.0
SG A:CYS221 2.3 14.0 1.0
O32 A:BMH2 2.4 17.7 1.0
C31 A:BMH2 3.1 18.6 1.0
CE1 A:HIS263 3.1 15.8 1.0
C3 A:BMH2 3.1 18.1 1.0
CG A:ASP120 3.1 14.5 1.0
CD2 A:HIS263 3.2 18.7 1.0
C5 A:BMH2 3.3 19.9 1.0
CB A:CYS221 3.3 14.5 1.0
O A:HOH403 3.4 18.2 1.0
OD1 A:ASP120 3.5 15.1 1.0
C1 A:BMH2 3.8 18.4 1.0
C2 A:BMH2 3.8 17.2 1.0
NH2 A:ARG121 3.9 15.3 1.0
S21 A:BMH2 4.1 18.8 1.0
ND1 A:HIS263 4.2 15.0 1.0
O62 A:BMH2 4.2 18.5 1.0
CA A:CYS221 4.2 13.7 1.0
CG A:HIS263 4.3 14.7 1.0
O31 A:BMH2 4.4 17.9 1.0
CB A:ASP120 4.4 13.7 1.0
CE1 A:HIS196 4.4 15.8 1.0
C6 A:BMH2 4.4 18.2 1.0
CZ A:ARG121 4.6 13.3 1.0
NE A:ARG121 4.6 13.6 1.0
NE2 A:HIS196 4.8 14.9 1.0
N A:CYS221 5.0 13.7 1.0
C61 A:BMH2 5.0 19.5 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 Aug 20 00:13:26 2025

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