› 2srt

Solution NMR

CATALYTIC DOMAIN OF HUMAN STROMELYSIN-1 AT PH 5.5 AND 40OC COMPLEXED WITH INHIBITOR

Released:
DOI: 10.2210/pdb2srt/pdb
PDB entry 2srt coloured by chain, ensemble of 30 models, front view.
PDB entry 2srt coloured by chain, ensemble of 30 models, side view.
PDB entry 2srt coloured by chain, ensemble of 30 models, top view.
Source organism: Homo sapiens
Primary publication:
The NMR structure of the inhibited catalytic domain of human stromelysin-1.
Gooley PR, O'Connell JF, Marcy AI, Cuca GC, Salowe SP, Bush BL, Hermes JD, Esser CK, Hagmann WK, Springer JP
Nat Struct Biol 1 111-8 (1994)
PMID: 7656014

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 domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-530593 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Stromelysin-1 Chain: A
Molecule details ›
Chain: A
Length: 173 amino acids
Theoretical weight: 19.42 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P08254 (Residues: 100-272; Coverage: 38%)
Gene names: MMP3, STMY1
Sequence domains: Matrixin
Structure domains: Collagenase (Catalytic Domain)

Ligands and Environments

2 bound ligands:
Ligand ZN 2 x ZN
Ligand 8MI 1 x 8MI
No modified residues

Experiments and Validation Details

Entry percentile scores
Expression system: Escherichia coli

Quick links

Citations

13 review citations

Matrix metalloproteinases: structures, evolution, and diversification.
Massova et al. (1998)
12 more

2 mentions without citation

Conformational variability of matrix metalloproteinases: beyond a single 3D structure.
Bertini et al. (2005)
1 more