Structure of PDB 3i7g Chain B

Receptor sequence
>3i7gB (length=163) Species: 9606 (Homo sapiens) [Search protein sequence]
YNVFPRTLKWSKMNLTYRIVNYTPDMTHSEVEKAFKKAFKVWSDVTPLNF
TRLHDGIADIMISFGIKEHGDFYPFDGPSGLLAHAFPPGPNYGGDAHFDD
DETWTSSSKGYNLFLVAAHEFGHSLGLDHSKDPGALMFPIYTYSHFMLPD
DDVQGIQSLYGPG
3D structure
PDB3i7g Improving potency and selectivity of a new class of non-Zn-chelating MMP-13 inhibitors.
ChainB
Resolution1.95 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H222 E223 H226 H232
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 H222 H226 H232 H119 H123 H129
BS02 ZN B H172 D174 H187 H200 H69 D71 H84 H97
BS03 CA B D128 D203 E205 D25 D100 E102
BS04 CA B D179 G180 S182 L184 D202 E205 D76 G77 S79 L81 D99 E102
BS05 CA B D162 N194 Y195 G196 D198 D59 N91 Y92 G93 D95
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:3i7g, PDBe:3i7g, PDBj:3i7g
PDBsum3i7g
PubMed19692239
UniProtP45452|MMP13_HUMAN Collagenase 3 (Gene Name=MMP13)

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