› 2tcl

X-ray diffraction
2.2Å resolution

STRUCTURE OF THE CATALYTIC DOMAIN OF HUMAN FIBROBLAST COLLAGENASE COMPLEXED WITH AN INHIBITOR

Released:
DOI: 10.2210/pdb2tcl/pdb
PDB entry 2tcl coloured by chain, front view.
PDB entry 2tcl coloured by chain, side view.
PDB entry 2tcl coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structure of the catalytic domain of human fibroblast collagenase complexed with an inhibitor.
Borkakoti N, Winkler FK, Williams DH, D'Arcy A, Broadhurst MJ, Brown PA, Johnson WH, Murray EJ
Nat Struct Biol 1 106-10 (1994)
PMID: 7656013

Function and Biology Details

Reaction catalysed: 
Cleavage of the triple helix of collagen at about three-quarters of the length of the molecule from the N-terminus, at 775-Gly-|-Ile-776 in the alpha-1(I) chain. Cleaves synthetic substrates and alpha-macroglobulins at bonds where P1' is a hydrophobic residue.
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-137297 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
22 kDa interstitial collagenase Chain: A
Molecule details ›
Chain: A
Length: 169 amino acids
Theoretical weight: 18.87 KDa
Source organism: Homo sapiens
UniProt:
  • Canonical: P03956 (Residues: 101-269; Coverage: 38%)
Gene names: CLG, MMP1
Sequence domains: Matrixin
Structure domains: Collagenase (Catalytic Domain)

Ligands and Environments

4 bound ligands:
Ligand ZN 2 x ZN
Ligand SM 1 x SM
Ligand CA 2 x CA
Ligand RO4 1 x RO4
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: I4
Unit cell:
a: 86.96Å b: 86.96Å c: 40.96Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.162 0.162 not available

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Citations

19 review citations

Molecular determinants of metalloproteinase substrate specificity: matrix metalloproteinase substrate binding domains, modules, and exosites.
Overall CM. (2002)
18 more

9 mentions without citation

Peripheral membrane associations of matrix metalloproteinases.
Van Doren et al. (2017)
8 more