1ge7

X-ray diffraction
2Å resolution

ZINC PEPTIDASE FROM GRIFOLA FRONDOSA

Released:
Model geometry
Fit model/data

Function and Biology Details

Reaction catalysed:
Preferential cleavage in proteins: -Xaa-|-Lys- (in which Xaa may be Pro).
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-160476 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Peptidyl-Lys metalloendopeptidase Chains: A, B
Molecule details ›
Chains: A, B
Length: 167 amino acids
Theoretical weight: 18.06 KDa
Source organism: Grifola frondosa
UniProt:
  • Canonical: P81054 (Residues: 182-348; Coverage: 51%)
Gene name: MEP
Sequence domains: Lysine-specific metallo-endopeptidase
Structure domains: Collagenase (Catalytic Domain)

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL45XU
Spacegroup: P43
Unit cell:
a: 30.202Å b: 30.202Å c: 308.049Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.179 0.179 0.218