› 1gen

X-ray diffraction
2.15Å resolution

C-TERMINAL DOMAIN OF GELATINASE A

Released:
DOI: 10.2210/pdb1gen/pdb
PDB 1gen coloured by chain and viewed from the front.
PDB 1gen coloured by chain and viewed from the side.
PDB 1gen coloured by chain and viewed from the top.
Source organism: Homo sapiens
Primary publication:
Crystal structure of the haemopexin-like C-terminal domain of gelatinase A.
Libson AM, Gittis AG, Collier IE, Marmer BL, Goldberg GI, Lattman EE
Nat. Struct. Biol. 2 938-42 (1995)
PMID: 7583664

Function and Biology Details

Reaction catalysed: 
Cleavage of gelatin type I and collagen types IV, V, VII, X. Cleaves the collagen-like sequence Pro-Gln-Gly-|-Ile-Ala-Gly-Gln.
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
PEX Chain: A
Molecule details ›
Chain: A
Length: 218 amino acids
Theoretical weight: 24.66 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P08253 (Residues: 443-660; Coverage: 35%)
Gene names: CLG4A, MMP2
Sequence domains: Hemopexin
Structure domains: Hemopexin-like domain

Ligands and Environments

4 bound ligands:
Ligand ZN 1 x ZN
Ligand CA 1 x CA
Ligand CL 1 x CL
Ligand NA 1 x NA
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P212121
Unit cell:
a: 57.9Å b: 77.4Å c: 53.4Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.188 0.188 0.26
Expression system: Escherichia coli

Quick links

Citations

11 review citations

Progress in matrix metalloproteinase research.
Murphy et al. (2008)
10 more

10 mentions without citation

A unified statistical model to support local sequence order independent similarity searching for ligand-binding sites and its application to genome-based drug discovery.
Xie et al. (2009)
9 more