Structure of PDB 4dpe Chain B

Receptor sequence
>4dpeB (length=167) Species: 9606 (Homo sapiens) [Search protein sequence]
IPKWRKTHLTYRIVNYTPDLPKDAVDSAVEKALKVWEEVTPLTFSRLYEG
EADIMISFAVREHGDFYPFDGPGNVLAHAYAPGPGINGDAHFDDDEQWTK
DTTGTNLFLVAAHEIGHSLGLFHSANTEALMYPLYHSLTDLTRFRLSQDD
INGIQSLYGPPPDSPET
3D structure
PDB4dpe Structure of matrix metalloproteinase-3 with a platinum-based inhibitor.
ChainB
Resolution1.96 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) H113 E114 H117 H123
Enzyme Commision number 3.4.24.17: stromelysin 1.
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 H113 H117 H123
BS02 ZN B H151 D153 H166 H179 H63 D65 H78 H91
BS03 CA B D158 G159 G161 V163 D181 E184 D70 G71 G73 V75 D93 E96
BS04 CA B D141 G173 N175 D177 D53 G85 N87 D89
BS05 CA B D107 D182 E184 D19 D94 E96
BS06 PT B E139 M143 E51 M55
BS07 NGH B V163 L164 A165 H201 E202 H205 H211 Y223 V75 L76 A77 H113 E114 H117 H123 Y135 BindingDB: Ki=132nM,IC50=6500nM
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:4dpe, PDBe:4dpe, PDBj:4dpe
PDBsum4dpe
PubMed23660647
UniProtP08254|MMP3_HUMAN Stromelysin-1 (Gene Name=MMP3)

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