Structure of PDB 2ozr Chain D

Receptor sequence

>2ozrD (length=166) Species: 9606 (Homo sapiens)

NVFPRTLKWSKMNLTYRIVNYTPDMTHSEVEKAFKKAFKVWSDVTPLNFT
RLHDGIADIMISFGIKEHGDFYPFDGPSGLLAHAFPPGPNYGGDAHFDDD
ETWTSSSKGYNLFLVAAHEFGHSLGLDHSKDPGALMFPIYTYTGKSHFML
PDDDVQGIQSLYGPGD

3D structure

• PDB: 2ozr Discovery and characterization of a novel inhibitor of matrix metalloprotease-13 that reduces cartilage damage in vivo without joint fibroplasia side effects.
• Chain: D
• Resolution: 2.3 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): H201 E202 H205 H211
• Catalytic site (residue number reindexed from 1): H118 E119 H122 H128
• 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	D	H201 H205 H211	H118 H122 H128
BS02	ZN	D	H151 D153 H166 H179	H68 D70 H83 H96
BS03	CA	D	D158 G159 S161 L163 D181 E184	D75 G76 S78 L80 D98 E101
BS04	CA	D	D141 N173 G175 D177	D58 N90 G92 D94
BS05	CA	D	D107 D182 E184	D24 D99 E101
BS06	GG1	D	K119 F196 L197 H201 L218 F220 I222 Y223 Y225 T226 G227 K228 S229 F231 M232 P234	K36 F113 L114 H118 L135 F137 I139 Y140 Y142 T143 G144 K145 S146 F148 M149 P151	MOAD: ic50=0.67nM BindingDB: IC50=0.670000nM

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:2ozr, PDBe:2ozr, PDBj:2ozr
• PDBsum: 2ozr
• PubMed: 17623656
• UniProt: P45452|MMP13_HUMAN Collagenase 3 (Gene Name=MMP13)