› 1c8t

X-ray diffraction
2.6Å resolution

HUMAN STROMELYSIN-1 (E202Q) CATALYTIC DOMAIN COMPLEXED WITH RO-26-2812

Released:
DOI: 10.2210/pdb1c8t/pdb
PDB entry 1c8t coloured by chain, front view.
PDB entry 1c8t coloured by chain, side view.
PDB entry 1c8t coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Expression, characterization and structure determination of an active site mutant (Glu202-Gln) of mini-stromelysin-1.
Steele DL, El-Kabbani O, Dunten P, Windsor LJ, Kammlott RU, Crowther RL, Michoud C, Engler JA, Birktoft JJ
Protein Eng 13 397-405 (2000)
PMID: 10877850

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:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-140080 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Stromelysin-1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 167 amino acids
Theoretical weight: 18.69 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P08254 (Residues: 103-269; Coverage: 36%)
Gene names: MMP3, STMY1
Sequence domains: Matrixin
Structure domains: Collagenase (Catalytic Domain)

Ligands and Environments

3 bound ligands:
Ligand ZN 4 x ZN
Ligand CA 6 x CA
Ligand TR1 2 x TR1
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P212121
Unit cell:
a: 120.1Å b: 47Å c: 54.9Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.22 not available not available
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Future challenges facing the development of specific active-site-directed synthetic inhibitors of MMPs.
Cuniasse et al. (2005)
1 more

2 mentions without citation

Structural signatures of enzyme binding pockets from order-independent surface alignment: a study of metalloendopeptidase and NAD binding proteins.
Dundas et al. (2011)
1 more