› 2df5

X-ray diffraction
2.3Å resolution

Crystal Structure of Pf-PCP(1-204)-C

Released:
DOI: 10.2210/pdb2df5/pdb
PDB entry 2df5 coloured by chain, front view.
PDB entry 2df5 coloured by chain, side view.
PDB entry 2df5 coloured by chain, top view.
Source organism: Pyrococcus furiosus
Primary publication:
Conformational contagion in a protein: structural properties of a chameleon sequence.
Takano K, Katagiri Y, Mukaiyama A, Chon H, Matsumura H, Koga Y, Kanaya S
Proteins 68 617-25 (2007)
PMID: 17510955

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 analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-130730 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Pyrrolidone-carboxylate peptidase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 213 amino acids
Theoretical weight: 23.39 KDa
Source organism: Pyrococcus furiosus
Expression system: Escherichia coli
UniProt:
  • Canonical: O73944 (Residues: 1-206; Coverage: 99%)
Gene names: PF1299, pcp
Sequence domains: Pyroglutamyl peptidase
Structure domains: Peptidase C15, pyroglutamyl peptidase I-like

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL44XU
Spacegroup: P21
Unit cell:
a: 104.24Å b: 104.45Å c: 48.25Å
α: 90° β: 100.39° γ: 90°
R-values:
R R work R free
0.197 0.197 0.234
Expression system: Escherichia coli

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Citations

2 review citations

Slow unfolding of monomeric proteins from hyperthermophiles with reversible unfolding.
Mukaiyama et al. (2009)
1 more