› 4f8z

X-ray diffraction
1.38Å resolution

Carboxypeptidase T with Boc-Leu

Released:
DOI: 10.2210/pdb4f8z/pdb
PDB entry 4f8z coloured by chain, front view.
PDB entry 4f8z coloured by chain, side view.
PDB entry 4f8z coloured by chain, top view.
Source organism: Thermoactinomyces vulgaris
Primary publication:
Three-dimensional structure of carboxypeptidase T from Thermoactinomyces vulgaris in complex with N-BOC-L-leucine.
Timofeev VI, Kuznetsov SA, Akparov VKh, Chestukhina GG, Kuranova IP
Biochemistry (Mosc) 78 252-9 (2013)
PMID: 23586718

Function and Biology Details

Reaction catalysed: 
Releases a C-terminal residue, which may be hydrophobic or positively charged.
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-151339 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Carboxypeptidase T Chain: A
Molecule details ›
Chain: A
Length: 323 amino acids
Theoretical weight: 36.64 KDa
Source organism: Thermoactinomyces vulgaris
Expression system: Escherichia coli
UniProt:
  • Canonical: P29068 (Residues: 99-421; Coverage: 81%)
Gene name: cpt
Sequence domains: Zinc carboxypeptidase
Structure domains: Zn peptidases

Ligands and Environments

5 bound ligands:
Ligand ZN 1 x ZN
Ligand BL2 1 x BL2
Ligand SO4 3 x SO4
Ligand CA 4 x CA
Ligand GOL 22 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL41XU
Spacegroup: P6322
Unit cell:
a: 157.914Å b: 157.914Å c: 104.068Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.14 0.139 0.152
Expression system: Escherichia coli

Quick links

Citations

1 citations in other articles

Structural insights into the broad substrate specificity of carboxypeptidase T from Thermoactinomyces vulgaris.
Akparov et al. (2015)