PDBsum entry 7llh

Hydrolase/antibiotic

PDB id: 7llh

Contents

Protein chains

260 a.a.

Ligands

IM2 ×2

Waters ×129

PDB id:

7llh

Name:

Hydrolase/antibiotic

Title:

Kpc-2 f72y mutant with acylated imipenem

Structure:

Carbapenem-hydrolyzing beta-lactamase kpc. Chain: a, b. Synonym: carbapenem-hydrolyzing beta-lactamase kpc-1. Engineered: yes. Mutation: yes

Source:

Klebsiella pneumoniae. Organism_taxid: 573. Gene: bla, kpc, kpc1. Expressed in: escherichia coli. Expression_system_taxid: 562

Resolution:

2.10Å R-factor: 0.184 R-free: 0.219

Authors:

I.Furey,T.Palzkill,B.Sankaran,L.Hu,B.V.V.Prasad

Key ref:

i.m.furey and t.palzkill (2021). Local Interactions with the Glu166 Base and the Conformation of an Active Site Loop Play Key Roles in Carbapenem Hydrolysis by the KPC-2 beta-lactamase. J.Biol.Chem., 0, 100799-100799. PubMed id: 34022225

Date:

03-Feb-21 Release date: 26-May-21

Protein chains

Q9F663  (BLKPC_KLEPN) -  Carbapenem-hydrolyzing beta-lactamase KPC from Klebsiella pneumoniae

Seq: 293 a.a.

Struc: 260 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+)

J.Biol.Chem. 0:100799-100799 (2021)

PubMed id: 34022225

Local Interactions with the Glu166 Base and the Conformation of an Active Site Loop Play Key Roles in Carbapenem Hydrolysis by the KPC-2 beta-lactamase.

i.m.furey, t.palzkill.

ABSTRACT

No abstract given.