› 1a2z

X-ray diffraction
1.73Å resolution

PYRROLIDONE CARBOXYL PEPTIDASE FROM THERMOCOCCUS LITORALIS

Released:
DOI: 10.2210/pdb1a2z/pdb
PDB entry 1a2z coloured by chain, front view.
PDB entry 1a2z coloured by chain, side view.
PDB entry 1a2z coloured by chain, top view.
Source organism: Thermococcus litoralis
Primary publication:
X-ray structure of pyrrolidone carboxyl peptidase from the hyperthermophilic archaeon Thermococcus litoralis.
Singleton M, Isupov M, Littlechild J
Structure 7 237-44 (1999)
PMID: 10368293

Function and Biology Details

Reaction catalysed: 
Release of an N-terminal pyroglutamyl group from a polypeptide, the second amino acid generally not being Pro.
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-126610 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Pyrrolidone-carboxylate peptidase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 220 amino acids
Theoretical weight: 24.78 KDa
Source organism: Thermococcus litoralis
Expression system: Escherichia coli
UniProt:
  • Canonical: O07883 (Residues: 1-220; Coverage: 100%)
Gene names: OCC_03923, pcp
Sequence domains: Pyroglutamyl peptidase
Structure domains: Peptidase C15, pyroglutamyl peptidase I-like

Ligands and Environments

1 bound ligand:
Ligand SO4 4 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X11
Spacegroup: P21212
Unit cell:
a: 91.644Å b: 147.01Å c: 71.553Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.18 0.18 0.22
Expression system: Escherichia coli

Quick links

Citations

4 review citations

Metal and redox modulation of cysteine protein function.
Giles et al. (2003)
3 more

7 mentions without citation

Enzymes from Extreme Environments and Their Industrial Applications.
Littlechild JA. (2015)
6 more