› 830c

X-ray diffraction
1.6Å resolution

COLLAGENASE-3 (MMP-13) COMPLEXED TO A SULPHONE-BASED HYDROXAMIC ACID

Released:
DOI: 10.2210/pdb830c/pdb
PDB entry 830c coloured by chain, front view.
PDB entry 830c coloured by chain, side view.
PDB entry 830c coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystal structures of MMP-1 and -13 reveal the structural basis for selectivity of collagenase inhibitors.
Lovejoy B, Welch AR, Carr S, Luong C, Broka C, Hendricks RT, Campbell JA, Walker KA, Martin R, Van Wart H, Browner MF
Nat Struct Biol 6 217-21 (1999)
PMID: 10074939

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-155286 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Collagenase 3 Chains: A, B
Molecule details ›
Chains: A, B
Length: 168 amino acids
Theoretical weight: 18.91 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P45452 (Residues: 104-271; Coverage: 37%)
Gene name: MMP13
Sequence domains: Matrixin
Structure domains: Collagenase (Catalytic Domain)

Ligands and Environments

3 bound ligands:
Ligand ZN 4 x ZN
Ligand CA 2 x CA
Ligand RS1 2 x RS1
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.2
Spacegroup: C2
Unit cell:
a: 136.072Å b: 36.098Å c: 96.368Å
α: 90° β: 131.06° γ: 90°
R-values:
R R work R free
0.208 0.208 0.266
Expression system: Escherichia coli

Quick links

Citations

19 review citations

Implications of protein flexibility for drug discovery.
Teague SJ. (2003)
18 more

20 mentions without citation

Genetic insights into non-syndromic Tetralogy of Fallot.
Althali et al. (2022)
19 more