Structure of PDB 2ozr Chain C

Receptor sequence

>2ozrC (length=167) Species: 9606 (Homo sapiens)

YNVFPRTLKWSKMNLTYRIVNYTPDMTHSEVEKAFKKAFKVWSDVTPLNF
TRLHDGIADIMISFGIKEHGDFYPFDGPSGLLAHAFPPGPNYGGDAHFDD
DETWTSSSKGYNLFLVAAHEFGHSLGLDHSKDPGALMFPIYTYTGKSHFM
LPDDDVQGIQSLYGPGD

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: C
• Resolution: 2.3 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): H201 E202 H205 H211
• 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	C	H201 H205 H211	H119 H123 H129
BS02	ZN	C	H151 D153 H166 H179	H69 D71 H84 H97
BS03	CA	C	D158 G159 S161 L163 D181 E184	D76 G77 S79 L81 D99 E102
BS04	CA	C	D141 N173 G175 D177	D59 N91 G93 D95
BS05	CA	C	D107 D182 E184	D25 D100 E102
BS06	GG1	C	K119 F196 L197 H201 L218 F220 I222 Y223 Y225 T226 S229 F231	K37 F114 L115 H119 L136 F138 I140 Y141 Y143 T144 S147 F149	MOAD: ic50=0.67nM PDBbind-CN: -logKd/Ki=9.17,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)