Structure analysis

Solution Structure of matrix metalloproteinase 12 (MMP12) in the presence of N-Isobutyl-N-[4-methoxyphenylsulfonyl]glycyl hydroxamic acid (NNGH)

Solution NMR
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: 8894.48 Å2
Buried surface area: 858.78 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

Chain: A
Length: 159 amino acids
Theoretical weight: 17.62 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)
SCOP: Matrix metalloproteases, catalytic domain
PDBe-KB: UniProt Coverage View: P39900  
115920406080100120140
 
50100150
UniProt
P39900
Chains
Domains
Secondary structure
Flexibility predictions
Early folding residue predictions
Ligand binding sites

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