Structure analysis

Crystal structure of the catalytic domain of MMP-12 in complex with a selective sugar-conjugated thiourea-linked carboxylate zinc-chelator water-soluble inhibitor (DC31).

X-ray diffraction
2.17Å resolution
Source organism: Homo sapiens
Assembly composition:
monomeric (preferred)
Entry contents: 1 distinct polypeptide molecule

Assemblies

Assembly 1
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Multimeric state: monomeric
Accessible surface area: 8133.83 Å2
Buried surface area: 701.38 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-153971
Assembly 2 (preferred)
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Multimeric state: monomeric
Accessible surface area: 8080.78 Å2
Buried surface area: 959.02 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-153971
Assembly 3
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Multimeric state: monomeric
Accessible surface area: 7913.51 Å2
Buried surface area: 659.18 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-153971
Assembly 4
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Multimeric state: monomeric
Accessible surface area: 8297.32 Å2
Buried surface area: 394.33 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-153971

Macromolecules

Chains: A, B, C, D
Length: 159 amino acids
Theoretical weight: 17.61 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P39900 (Residues: 106-263; Coverage: 35%)
Gene names: HME, MMP12
Pfam: Matrixin
InterPro:
CATH: Collagenase (Catalytic Domain)

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