› 1ge5

X-ray diffraction
2Å resolution

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
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-160475 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Peptidyl-Lys metalloendopeptidase Chain: A
Molecule details ›
Chain: A
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:
Ligand MAN 1 x MAN
Ligand ZN 1 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P1
Unit cell:
a: 30.8Å b: 40.5Å c: 30.5Å
α: 105.9° β: 91.7° γ: 103.5°
R-values:
R R work R free
0.184 0.184 0.222

Quick links

Citations

2 review citations

Structural aspects of the metzincin clan of metalloendopeptidases.
Gomis-Rüth FX. (2003)
1 more

1 mention without citation

Bovine herpesvirus 5 glycoprotein E is important for neuroinvasiveness and neurovirulence in the olfactory pathway of the rabbit.
Chowdhury et al. (2000)