› 5wvu

X-ray diffraction
2.6Å resolution

Crystal structure of carboxypeptidase from Thermus thermophilus

Released:
DOI: 10.2210/pdb5wvu/pdb
PDB entry 5wvu coloured by chain, front view.
PDB entry 5wvu coloured by chain, side view.
PDB entry 5wvu coloured by chain, top view.
Source organism: Thermus thermophilus HB8
Primary publication:
Insight into the transition between the open and closed conformations of Thermus thermophilus carboxypeptidase.
Okai M, Yamamura A, Hayakawa K, Tsutsui S, Miyazono KI, Lee WC, Nagata K, Inoue Y, Tanokura M
Biochem Biophys Res Commun 484 787-793 (2017)
PMID: 28161633

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
Sequence domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-178184 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Thermostable carboxypeptidase 1 Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 510 amino acids
Theoretical weight: 58.09 KDa
Source organism: Thermus thermophilus HB8
Expression system: Escherichia coli
UniProt:
  • Canonical: Q5SLM3 (Residues: 1-510; Coverage: 100%)
Gene name: TTHA0270
Sequence domains: Carboxypeptidase Taq (M32) metallopeptidase
Structure domains: Neurolysin; domain 3

Ligands and Environments

2 bound ligands:
Ligand GOL 4 x GOL
Ligand ZN 3 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE AR-NW12A
Spacegroup: C2221
Unit cell:
a: 170.1Å b: 233.7Å c: 124.4Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.192 0.19 0.234
Expression system: Escherichia coli

Quick links

Citations

2 citation in other articles

Potent and selective inhibitors for M32 metallocarboxypeptidases identified from high-throughput screening of anti-kinetoplastid chemical boxes.
Salas-Sarduy et al. (2019)
1 more

2 mentions without citation

From Data Mining of Chitinophaga sp. Genome to Enzyme Discovery of a Hyperthermophilic Metallocarboxypeptidase.
Fernandes et al. (2021)
1 more