Structure analysis

Crystal structure of the catalytic domain of MMP-13 complexed with N-(3-methoxybenzyl)-4-oxo-3,4-dihydrothieno[2,3-d]pyrimidine-2-carboxamide

X-ray diffraction
1.6Å resolution
Source organism: Homo sapiens
Assemblies composition:
monomeric (preferred)
homo dimer
Entry contents: 1 distinct polypeptide molecule

Assemblies

Assembly 1 (preferred)
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Multimeric state: monomeric
Accessible surface area: 9516.59 Å2
Buried surface area: 734.88 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: 9208.13 Å2
Buried surface area: 728.03 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 3
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Multimeric state: homo dimer
Accessible surface area: 16291.22 Å2
Buried surface area: 3896.42 Å2
Dissociation area: 1,303.25 Å2
Dissociation energy (ΔGdiss): 6.16 kcal/mol
Dissociation entropy (TΔSdiss): 11.89 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-155288

Macromolecules

Chains: A, B
Length: 171 amino acids
Theoretical weight: 19.24 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P45452 (Residues: 104-274; Coverage: 38%)
Gene name: MMP13
Pfam: Matrixin
InterPro:
CATH: Collagenase (Catalytic Domain)

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