› 2p74

X-ray diffraction
0.88Å resolution

CTX-M-9 class A beta-lactamase apo crystal structure at 0.88 Angstrom resolution

Released:
DOI: 10.2210/pdb2p74/pdb
PDB entry 2p74 coloured by chain, front view.
PDB entry 2p74 coloured by chain, side view.
PDB entry 2p74 coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
The acylation mechanism of CTX-M beta-lactamase at 0.88 a resolution.
Chen Y, Bonnet R, Shoichet BK
J Am Chem Soc 129 5378-80 (2007)
PMID: 17408273

Function and Biology Details

Reaction catalysed: 
A beta-lactam + H(2)O = a substituted beta-amino acid
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-192212 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Beta-lactamase Chains: A, B
Molecule details ›
Chains: A, B
Length: 263 amino acids
Theoretical weight: 27.96 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9L5C8 (Residues: 29-291; Coverage: 100%)
Gene names: RCS51_P0174, bla CTX-M-9, blaCTX-M-9, blaCTX-M-9a, blaCTX-M-9b
Sequence domains:
Structure domains: DD-peptidase/beta-lactamase superfamily

Ligands and Environments

2 bound ligands:
Ligand PO4 5 x PO4
Ligand K 2 x K
1 modified residue:
Ligand PCA 2 x PCA

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.3.1
Spacegroup: P21
Unit cell:
a: 45.162Å b: 106.796Å c: 47.785Å
α: 90° β: 102.09° γ: 90°
R-values:
R R work R free
0.1 0.1 0.114
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

7 review citations

β-Lactamases and β-Lactamase Inhibitors in the 21st Century.
Tooke et al. (2019)
6 more

10 mentions without citation

The acylation mechanism of CTX-M beta-lactamase at 0.88 a resolution.
Chen et al. (2007)
9 more