Structure analysis

Crystal Structure of Human MMP-13 complexed with a (pyridin-4-yl)-2H-tetrazole compound

X-ray diffraction
1.97Å resolution
Source organism: Homo sapiens
Assembly composition:
monomeric (preferred)
Entry contents: 1 distinct polypeptide molecule

Assemblies

Assembly 1 (preferred)
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Multimeric state: monomeric
Accessible surface area: 9067.85 Å2
Buried surface area: 288.9 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-155286
Assembly 2
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Multimeric state: monomeric
Accessible surface area: 8192.02 Å2
Buried surface area: 277.95 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-155286

Macromolecules

Chains: A, B
Length: 167 amino acids
Theoretical weight: 18.78 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P45452 (Residues: 104-270; Coverage: 37%)
Gene name: MMP13
Pfam: Matrixin
InterPro:
CATH: Collagenase (Catalytic Domain)

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