Structure of PDB 2ow0 Chain B

Receptor sequence

>2ow0B (length=155) Species: 9606 (Homo sapiens)

LKWHHHNITYWIQNYSEDLPRAVIDDAFARAFALWSAVTPLTFTRVYSRD
ADIVIQFGVAEHGDGYPFDGKDGLLAHAFPPGPGIQGDAHFDDDELWSLG
KGQGYSLFLVAAHQFGHALGLDHSSVPEALMYPMYRFTEGPPLHKDDVNG
IRHLY

3D structure

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

Enzymatic activity

• Catalytic site (original residue number in PDB): H401 Q402 H405 H411
• Catalytic site (residue number reindexed from 1): H113 Q114 H117 H123
• 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	B	H401 H405 H411	H113 H117 H123
BS02	ZN	B	H175 D177 H190 H203	H62 D64 H77 H90
BS03	CA	B	D165 G197 Q199 D201	D52 G84 Q86 D88
BS04	CA	B	D182 G183 D185 L187 D205 E208	D69 G70 D72 L74 D92 E95
BS05	CA	B	D131 D206 E208	D18 D93 E95
BS06	CA	B	S149 T152	S36 T39
BS07	6MR	B	L188 A189 H401 Q402 H405 H411 L418 Y420 P421 M422 Y423	L75 A76 H113 Q114 H117 H123 L130 Y132 P133 M134 Y135

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)