› 1jap

X-ray diffraction
1.82Å resolution

COMPLEX OF PRO-LEU-GLY-HYDROXYLAMINE WITH THE CATALYTIC DOMAIN OF MATRIX METALLO PROTEINASE-8 (MET80 FORM)

Released:
DOI: 10.2210/pdb1jap/pdb
PDB entry 1jap coloured by chain, front view.
PDB entry 1jap coloured by chain, side view.
PDB entry 1jap coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
The X-ray crystal structure of the catalytic domain of human neutrophil collagenase inhibited by a substrate analogue reveals the essentials for catalysis and specificity.
Bode W, Reinemer P, Huber R, Kleine T, Schnierer S, Tschesche H
EMBO J 13 1263-9 (1994)
PMID: 8137810

Function and Biology Details

Reaction catalysed: 
Cleavage of interstitial collagens in the triple helical domain. Unlike EC 3.4.24.7, this enzyme cleaves type III collagen more slowly than type I.
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-149834 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Neutrophil collagenase Chain: A
Molecule details ›
Chain: A
Length: 163 amino acids
Theoretical weight: 18.11 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P22894 (Residues: 100-262; Coverage: 37%)
Gene names: CLG1, MMP8
Sequence domains: Matrixin
Structure domains: Collagenase (Catalytic Domain)
PRO-LEU-GLY-HYDROXYLAMINE Chain: I
Molecule details ›
Chain: I
Length: 4 amino acids
Theoretical weight: 300 Da
Source organism: Homo sapiens
Expression system: Not provided

Ligands and Environments

2 bound ligands:
Ligand CA 2 x CA
Ligand ZN 2 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P212121
Unit cell:
a: 33.09Å b: 69.37Å c: 72.48Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.194 0.194 not available
Expression systems:
  • Escherichia coli
  • Not provided

Quick links

Citations

41 review citations

The metzincins--topological and sequential relations between the astacins, adamalysins, serralysins, and matrixins (collagenases) define a superfamily of zinc-peptidases.
Stöcker et al. (1995)
40 more

5 mentions without citation

A comparison of the binding sites of matrix metalloproteinases and tumor necrosis factor-alpha converting enzyme: implications for selectivity.
Lukacova et al. (2005)
4 more