Structure of PDB 1eub Chain A

Receptor sequence

>1eubA (length=171) Species: 9606 (Homo sapiens)

YNVFPRTLKWSKMNLTYRIVNYTPDMTHSEVEKAFKKAFKVWSDVTPLNF
TRLHDGIADIMISFGIKEHGDFYPFDGPSGLLAHAFPPGPNYGGDAHFDD
DETWTSSSKGYNLFLVAAHEFGHSLGLDHSKDPGALMFPIYTYTGKSHFM
LPDDDVQGIQSLYGPGDEDPN

3D structure

• 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.
• Chain: A
• Resolution: N/A

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.-

Interaction with ligand

Site #	Ligand	Ligand chain	Binding residues on receptor (original residue number in PDB)	Binding residues on receptor (residue number reindexed from 1)	Binding affinity
BS01	ZN	A	H172 H187 H200	H69 H84 H97
BS02	ZN	A	H222 H226 H232 M240	H119 H123 H129 M137
BS03	CA	A	D162 N194 Y195 G196 D198	D59 N91 Y92 G93 D95
BS04	CA	A	D179 G180 P181 S182 L184 D202 E205	D76 G77 P78 S79 L81 D99 E102
BS05	HAV	A	L184 A186 H222 E223 H226 H232	L81 A83 H119 E120 H123 H129	PDBbind-CN: -logKd/Ki=8.72,Ki=1.9nM
BS06	3MP	A	G183 P242	G80 P139	PDBbind-CN: -logKd/Ki=8.72,Ki=1.9nM
BS07	MSB	A	L185 A186 L218 H222 F241 P242 I243 Y244	L82 A83 L115 H119 F138 P139 I140 Y141	PDBbind-CN: -logKd/Ki=8.72,Ki=1.9nM

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)