PDBsum entry 4d1v

Hydrolase

PDB id: 4d1v

Contents

Protein chain

227 a.a.

Metals

_ZN ×2

Waters ×241

PDB id:

4d1v

Name:

Hydrolase

Title:

A f218y mutant of vim-7 from pseudomonas aeruginosa

Structure:

Metallo-b-lactamase. Chain: a. Synonym: metallo-beta-lactamase. Engineered: yes. Mutation: yes

Source:

Pseudomonas aeruginosa. Organism_taxid: 287. Expressed in: escherichia coli. Expression_system_taxid: 469008. Expression_system_variant: rosetta 2 plyss

Resolution:

1.70Å R-factor: 0.161 R-free: 0.197

Authors:

H.-K.S.Leiros,S.Skagseth,K.S.W.Edvardsen,M.S.Lorentzen,G.E.K.Bjerga, I.Leiros,O.Samuelsen

Key ref:

H.K.Leiros et al. (2014). His224 alters the R2 drug binding site and Phe218 influences the catalytic efficiency of the metallo-β-lactamase VIM-7. Antimicrob Agents Chemother, 58, 4826-4836. PubMed id: 24913158 DOI: 10.1128/AAC.02735-13

Date:

05-May-14 Release date: 25-Jun-14

Protein chain

Q840P9  (Q840P9_PSEAI) -  beta-lactamase from Pseudomonas aeruginosa

Seq: 265 a.a.

Struc: 227 a.a.*

* PDB and UniProt seqs differ at 1 residue position (black cross)

Enzyme reactions

• Enzyme class: E.C.3.5.2.6 - beta-lactamase.
• Pathway: Penicillin Biosynthesis and Metabolism
• Reaction: a beta-lactam + H2O = a substituted beta-amino acid
• Cofactor: Zn(2+)

DOI no: 10.1128/AAC.02735-13

Antimicrob Agents Chemother 58:4826-4836 (2014)

PubMed id: 24913158

His224 alters the R2 drug binding site and Phe218 influences the catalytic efficiency of the metallo-β-lactamase VIM-7.

H.K.Leiros, S.Skagseth, K.S.Edvardsen, M.S.Lorentzen, G.E.Bjerga, I.Leiros, Ã.˜.Samuelsen.

ABSTRACT

No abstract given.