› 1gec

X-ray diffraction
2.1Å resolution

GLYCYL ENDOPEPTIDASE-COMPLEX WITH BENZYLOXYCARBONYL-LEUCINE-VALINE-GLYCINE-METHYLENE COVALENTLY BOUND TO CYSTEINE 25

Released:
DOI: 10.2210/pdb1gec/pdb
PDB entry 1gec coloured by chain, front view.
PDB entry 1gec coloured by chain, side view.
PDB entry 1gec coloured by chain, top view.
Source organism: Carica papaya
Primary publication:
Crystal structure of glycyl endopeptidase from Carica papaya: a cysteine endopeptidase of unusual substrate specificity.
O'Hara BP, Hemmings AM, Buttle DJ, Pearl LH
Biochemistry 34 13190-5 (1995)
PMID: 7548082

Function and Biology Details

Reaction catalysed: 
Preferential cleavage: Gly-|-, in proteins and small molecule substrates.
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-138850 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Papaya proteinase 4 Chain: E
Molecule details ›
Chain: E
Length: 216 amino acids
Theoretical weight: 23.34 KDa
Source organism: Carica papaya
UniProt:
  • Canonical: P05994 (Residues: 133-348; Coverage: 66%)
Sequence domains: Papain family cysteine protease
Structure domains: Cysteine proteinases
BENZYLOXYCARBONYL-LEUCINE-VALINE-GLYCINE-METHYLENE INHIBITOR Chain: I
Molecule details ›
Chain: I
Length: 5 amino acids
Theoretical weight: 464 Da
Source organism: Carica papaya
Expression system: Not provided

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P31
Unit cell:
a: 55.78Å b: 55.78Å c: 64.43Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.196 0.196 0.258
Expression system: Not provided

Quick links

Citations

5 review citations

The lysosomal cysteine proteases.
McGrath ME. (1999)
4 more

5 mentions without citation

The crystal structure of Pseudomonas avirulence protein AvrPphB: a papain-like fold with a distinct substrate-binding site.
Zhu et al. (2004)
4 more