› 1slm

X-ray diffraction
1.9Å resolution

CRYSTAL STRUCTURE OF FIBROBLAST STROMELYSIN-1: THE C-TRUNCATED HUMAN PROENZYME

Released:
DOI: 10.2210/pdb1slm/pdb
PDB entry 1slm coloured by chain, front view.
PDB entry 1slm coloured by chain, side view.
PDB entry 1slm coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Stromelysin-1: three-dimensional structure of the inhibited catalytic domain and of the C-truncated proenzyme.
Becker JW, Marcy AI, Rokosz LL, Axel MG, Burbaum JJ, Fitzgerald PM, Cameron PM, Esser CK, Hagmann WK, Hermes JD
Protein Sci 4 1966-76 (1995)
PMID: 8535233

Function and Biology Details

Reaction catalysed: 
Preferential cleavage where P1', P2' and P3' are hydrophobic residues.
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-140080 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Stromelysin-1 Chain: A
Molecule details ›
Chain: A
Length: 255 amino acids
Theoretical weight: 28.82 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P08254 (Residues: 18-272; Coverage: 55%)
Gene names: MMP3, STMY1
Sequence domains:
Structure domains: Collagenase (Catalytic Domain)

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH2R
Spacegroup: F222
Unit cell:
a: 111.04Å b: 145.56Å c: 76.75Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.218 0.218 0.256
Expression system: Escherichia coli

Quick links

Citations

39 review citations

Matrix metalloproteinases and tissue inhibitors of metalloproteinases: structure, function, and biochemistry.
Visse et al. (2003)
38 more

15 mentions without citation

Annotation in three dimensions. PINTS: Patterns in Non-homologous Tertiary Structures.
Stark et al. (2003)
14 more