› 6m5p

X-ray diffraction
1.25Å resolution

A class C beta-lactamase

Released:
DOI: 10.2210/pdb6m5p/pdb
PDB entry 6m5p coloured by chain, front view.
PDB entry 6m5p coloured by chain, side view.
PDB entry 6m5p coloured by chain, top view.
Source organism: Klebsiella pneumoniae
Primary publication:
Novel inhibition mechanism of carbapenems on the ACC-1 class C β-lactamase.
Bae DW, Jung YE, Jeong BG, Cha SS
Arch Biochem Biophys 693 108570 (2020)
PMID: 32888908

Function and Biology Details

Reaction catalysed: 
A beta-lactam + H(2)O = a substituted beta-amino acid
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-194978 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Beta-lactamase Chain: A
Molecule details ›
Chain: A
Length: 370 amino acids
Theoretical weight: 40.7 KDa
Source organism: Klebsiella pneumoniae
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9XB24 (Residues: 24-386; Coverage: 100%)
Gene names: acc-1, bla-ACC-1
Sequence domains: Beta-lactamase

Ligands and Environments

1 bound ligand:
Ligand MER 1 x MER
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PAL/PLS BEAMLINE 5C (4A)
Spacegroup: C2
Unit cell:
a: 129.918Å b: 60.233Å c: 54.518Å
α: 90° β: 110.71° γ: 90°
R-values:
R R work R free
0.174 0.174 not available
Expression system: Escherichia coli

Quick links

Citations

2 review citations

β-Lactam antibiotic targets and resistance mechanisms: from covalent inhibitors to substrates.
Mora-Ochomogo et al. (2021)
1 more