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X-RAY STRUCTURE OF HUMAN STROMELYSIN CATALYTIC DOMAIN COMPLEXED WITH NON-PEPTIDE INHIBITORS: IMPLICATIONS FOR INHIBITOR SELECTIVITY

X-ray diffraction
2Å resolution
PDB entry 1b8y coloured by chain, front view.
PDB entry 1b8y coloured by chain, side view.
PDB entry 1b8y coloured by chain, top view.
Source organism: Homo sapiens
Assemblies composition:
monomeric (preferred)
homo dimer
Entry contents: 1 distinct polypeptide molecule

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Assemblies

Assembly 1 (preferred)
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Assembly Name: Stromelysin-1
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Multimeric state: monomeric
Accessible surface area: 8285.42 Å2
Buried surface area: 1244.82 Å2
Dissociation area: 0 Å2
Dissociation energy (ΔGdiss): 0 kcal/mol
Dissociation entropy (TΔSdiss): 0 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-140079
Assembly 2
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Assembly Name: Stromelysin-1
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Multimeric state: homo dimer
Accessible surface area: 14937.76 Å2
Buried surface area: 4127.71 Å2
Dissociation area: 888.45 Å2
Dissociation energy (ΔGdiss): 22.33 kcal/mol
Dissociation entropy (TΔSdiss): 13.82 kcal/mol
Symmetry number: 2
PDBe Complex ID: PDB-CPX-140080

Macromolecules

Stromelysin-1
Chain: A
Length: 167 amino acids
Theoretical weight: 18.79 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P08254 (Residues: 100-266; Coverage: 36%)
Gene names: MMP3, STMY1
Pfam: Matrixin
InterPro:
CATH: Collagenase (Catalytic Domain)
SCOP: Matrix metalloproteases, catalytic domain
Stromelysin-1 in PDB entry 1b8y, assembly 1, front view.
Stromelysin-1 in PDB entry 1b8y, assembly 1, side view.
Stromelysin-1 in PDB entry 1b8y, assembly 1, top view.
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