Structure of PDB 1eub Chain A Binding Site BS07

Receptor Information

>1eub Chain A (length=171) Species: 9606 (Homo sapiens)

YNVFPRTLKWSKMNLTYRIVNYTPDMTHSEVEKAFKKAFKVWSDVTPLNF
TRLHDGIADIMISFGIKEHGDFYPFDGPSGLLAHAFPPGPNYGGDAHFDD
DETWTSSSKGYNLFLVAAHEFGHSLGLDHSKDPGALMFPIYTYTGKSHFM
LPDDDVQGIQSLYGPGDEDPN

Ligand information

• Ligand ID: MSB
• InChI: InChI=1S/C7H8O3S/c1-10-6-2-4-7(5-3-6)11(8)9/h2-5,11H,1H3
• InChIKey: XUNSZADDFLWFOL-UHFFFAOYSA-N
• SMILES:
  : ether
  OpenEye OEToolkits 1.5.0: COc1ccc(cc1)S(=O)=O
  CACTVS 3.341: COc1ccc(cc1)[SH](=O)=O
• Formula: C7 H8 O3 S
• Name: 1-METHYLOXY-4-SULFONE-BENZENE
• ZINC: ZINC000150339282
• PDB chain: 1eub Chain A Residue 3

Receptor-Ligand Complex Structure

Structure summary

• PDB: 1eub Solution structure of the catalytic domain of human collagenase-3 (MMP-13) complexed to a potent non-peptidic sulfonamide inhibitor: binding comparison with stromelysin-1 and collagenase-1.
• Resolution: N/A
• Binding residue (original residue number in PDB): L185 A186 L218 H222 F241 P242 I243 Y244
• Binding residue (residue number reindexed from 1): L82 A83 L115 H119 F138 P139 I140 Y141
• Annotation score: 1
• Binding affinity: PDBbind-CN: -logKd/Ki=8.72,Ki=1.9nM

Enzymatic activity

• Catalytic site (original residue number in PDB): H222 E223 H226 H232
• Catalytic site (residue number reindexed from 1): H119 E120 H123 H129
• Enzyme Commision number: 3.4.24.-

Gene Ontology

Molecular Function

• GO:0004222 metalloendopeptidase activity
• GO:0008237 metallopeptidase activity
• GO:0008270 zinc ion binding

Biological Process

• GO:0006508 proteolysis

Cellular Component

• GO:0031012 extracellular matrix

External links

• PDB: RCSB:1eub, PDBe:1eub, PDBj:1eub
• PDBsum: 1eub
• PubMed: 10926524
• UniProt: P45452|MMP13_HUMAN Collagenase 3 (Gene Name=MMP13)