Structure analysis

CRYSTAL STRUCTURE OF THE CATALYTIC DOMAIN OF HUMAN FIBROBLAST STROMELYSIN-1 INHIBITED WITH THIADIAZOLE INHIBITOR PNU-142372

X-ray diffraction
1.8Å resolution
Source organism: Homo sapiens
Assemblies composition:
monomeric (preferred)
homo trimer
homo dimer
Entry contents: 1 distinct polypeptide molecule

Assemblies

Assembly 1 (preferred)
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Multimeric state: monomeric
Accessible surface area: 8678.0 Å2
Buried surface area: 1004.61 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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Multimeric state: homo trimer
Accessible surface area: 24952.71 Å2
Buried surface area: 3896.52 Å2
Dissociation area: 555.16 Å2
Dissociation energy (ΔGdiss): 23.9 kcal/mol
Dissociation entropy (TΔSdiss): 24.23 kcal/mol
Symmetry number: 3
PDBe Complex ID: PDB-CPX-140081
Assembly 3
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Multimeric state: homo dimer
Accessible surface area: 16116.53 Å2
Buried surface area: 3248.69 Å2
Dissociation area: 619.73 Å2
Dissociation energy (ΔGdiss): -5.45 kcal/mol
Dissociation entropy (TΔSdiss): 12.06 kcal/mol
Symmetry number: 2
PDBe Complex ID: PDB-CPX-140080

Macromolecules

Chain: A
Length: 165 amino acids
Theoretical weight: 18.6 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P08254 (Residues: 100-264; Coverage: 36%)
Gene names: MMP3, STMY1
Pfam: Matrixin
InterPro:
CATH: Collagenase (Catalytic Domain)
SCOP: Matrix metalloproteases, catalytic domain

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