3h3e

X-ray diffraction
2.75Å resolution

Crystal structure of Tm1679, A METAL-DEPENDENT HYDROLASE OF THE BETA-LACTAMASE SUPERFAMILY

Released:
Source organism: Thermotoga maritima
Entry authors: Cooper DR, Olekhnovitch N, Derewenda U, Derewenda ZS, Integrated Center for Structure and Function Innovation (ISFI)

Function and Biology Details

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-194854 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Metallo-beta-lactamase domain-containing protein Chain: A
Molecule details ›
Chain: A
Length: 267 amino acids
Theoretical weight: 30.49 KDa
Source organism: Thermotoga maritima
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9X207 (Residues: 2-255; Coverage: 100%)
Gene name: TM_1679
Sequence domains: Metallo-beta-lactamase superfamily
Structure domains: Ribonuclease Z/Hydroxyacylglutathione hydrolase-like

Ligands and Environments

1 bound ligand:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-BM
Spacegroup: P61
Unit cell:
a: 127.169Å b: 127.169Å c: 41.044Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.151 0.151 0.207
Expression system: Escherichia coli