Structure of PDB 2ow0 Chain A

Receptor sequence

>2ow0A (length=159) Species: 9606 (Homo sapiens)

FEGDLKWHHHNITYWIQNYSEDLPRAVIDDAFARAFALWSAVTPLTFTRV
YSRDADIVIQFGVAEHGDGYPFDGKDGLLAHAFPPGPGIQGDAHFDDDEL
WSLGKGQGYSLFLVAAHQFGHALGLDHSSVPEALMYPMYRFTEGPPLHKD
DVNGIRHLY

3D structure

• PDB: 2ow0 Crystal Structures of MMP-9 Complexes with Five Inhibitors: Contribution of the Flexible Arg424 Side-chain to Selectivity.
• Chain: A
• Resolution: 2.0 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): H401 Q402 H405 H411
• Catalytic site (residue number reindexed from 1): H117 Q118 H121 H127
• Enzyme Commision number: 3.4.24.35: gelatinase B.

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	H401 H405 H411	H117 H121 H127
BS02	ZN	A	H175 D177 H190 H203	H66 D68 H81 H94
BS03	CA	A	D165 G197 Q199 D201	D56 G88 Q90 D92
BS04	CA	A	D182 G183 D185 L187 D205 E208	D73 G74 D76 L78 D96 E99
BS05	CA	A	D131 D206 E208	D22 D97 E99
BS06	CA	A	S149 T152	S40 T43
BS07	6MR	A	E111 L188 A189 H401 Q402 H405 H411 L418 Y420 P421 M422 Y423	E2 L79 A80 H117 Q118 H121 H127 L134 Y136 P137 M138 Y139	PDBbind-CN: -logKd/Ki=6.70,IC50=201nM

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:2ow0, PDBe:2ow0, PDBj:2ow0
• PDBsum: 2ow0
• PubMed: 17599356
• UniProt: P14780|MMP9_HUMAN Matrix metalloproteinase-9 (Gene Name=MMP9)