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Solution NMR

SOLUTION STRUCTURE OF THE CATALYTIC FRAGMENT OF HUMAN COLLAGENASE-3 (MMP-13) COMPLEXED WITH A HYDROXAMIC ACID INHIBITOR

Released:
DOI: 10.2210/pdb1fls/pdb
PDB entry 1fls coloured by chain, front view.
PDB entry 1fls coloured by chain, side view.
PDB entry 1fls coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
High-resolution solution structure of the catalytic fragment of human collagenase-3 (MMP-13) complexed with a hydroxamic acid inhibitor.
Moy FJ, Chanda PK, Chen JM, Cosmi S, Edris W, Levin JI, Powers R
J Mol Biol 302 671-89 (2000)
PMID: 10986126

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 Chain: A
Molecule details ›
Chain: A
Length: 165 amino acids
Theoretical weight: 18.61 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P45452 (Residues: 104-268; Coverage: 37%)
Gene name: MMP13
Sequence domains: Matrixin
Structure domains: Collagenase (Catalytic Domain)

Ligands and Environments

3 bound ligands:
Ligand ZN 2 x ZN
Ligand CA 1 x CA
Ligand WAY 1 x WAY
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: distance geometry simulated annealing
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

3 mentions without citation

Bulbus Fritillariae Cirrhosae as a Respiratory Medicine: Is There a Potential Drug in the Treatment of COVID-19?
Quan et al. (2021)
2 more