X-ray diffraction
2.1Å resolution

Crystal structure of the Thermus thermophilus M32 carboxypeptidase


Function and Biology Details

Reaction catalysed:
Release of a C-terminal amino acid with broad specificity, except for -Pro.
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Metal-dependent carboxypeptidase Chains: A, B
Molecule details ›
Chains: A, B
Length: 509 amino acids
Theoretical weight: 58.03 KDa
Source organism: Thermus thermophilus HB27
Expression system: Escherichia coli
  • Canonical: Q72GY3 (Residues: 1-509; Coverage: 100%)
Gene name: TT_C1715
Sequence domains: Carboxypeptidase Taq (M32) metallopeptidase
Structure domains: Neurolysin; domain 3

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL1-5
Spacegroup: P21
Unit cell:
a: 58.61Å b: 84.33Å c: 109.05Å
α: 90° β: 93.75° γ: 90°
R R work R free
0.223 0.218 0.251
Expression system: Escherichia coli