Structure of PDB 2ozr Chain B

Receptor sequence
>2ozrB (length=167) Species: 9606 (Homo sapiens) [Search protein sequence]
YNVFPRTLKWSKMNLTYRIVNYTPDMTHSEVEKAFKKAFKVWSDVTPLNF
TRLHDGIADIMISFGIKEHGDFYPFDGPSGLLAHAFPPGPNYGGDAHFDD
DETWTSSSKGYNLFLVAAHEFGHSLGLDHSKDPGALMFPIYTYTGKSHFM
LPDDDVQGIQSLYGPGD
3D structure
PDB2ozr Discovery and characterization of a novel inhibitor of matrix metalloprotease-13 that reduces cartilage damage in vivo without joint fibroplasia side effects.
ChainB
Resolution2.3 Å
3D
structure
Catalytic site residues are labeled in the structure
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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 B H201 H205 H211 H119 H123 H129
BS02 ZN B H151 D153 H166 H179 H69 D71 H84 H97
BS03 CA B D158 G159 S161 L163 D181 E184 D76 G77 S79 L81 D99 E102
BS04 CA B D141 N173 Y174 G175 D177 D59 N91 Y92 G93 D95
BS05 CA B D107 D182 E184 D25 D100 E102
BS06 GG1 B N194 L197 H201 L218 F220 I222 Y223 Y225 T226 G227 S229 F231 N112 L115 H119 L136 F138 I140 Y141 Y143 T144 G145 S147 F149 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

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:2ozr, PDBe:2ozr, PDBj:2ozr
PDBsum2ozr
PubMed17623656
UniProtP45452|MMP13_HUMAN Collagenase 3 (Gene Name=MMP13)

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