Structure of PDB 1bqo Chain B

Receptor sequence
>1bqoB (length=173) Species: 9606 (Homo sapiens) [Search protein sequence]
FRTFPGIPKWRKTHLTYRIVNYTPDLPKDAVDSAVEKALKVWEEVTPLTF
SRLYEGEADIMISFAVREHGDFYPFDGPGNVLAHAYAPGPGINGDAHFDD
DEQWTKDTTGTNLFLVAAHEIGHSLGLFHSANTEALMYPLYHSLTDLTRF
RLSQDDINGIQSLYGPPPDSPET
3D structure
PDB1bqo Discovery of potent, achiral matrix metalloproteinase inhibitors.
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 3.4.24.17: 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 H119 H123 H129
BS02 ZN B H151 D153 H166 H179 H69 D71 H84 H97
BS03 CA B D158 G159 G161 V163 D181 E184 D76 G77 G79 V81 D99 E102
BS04 CA B D107 D182 E184 D25 D100 E102
BS05 CA B D141 G173 N175 D177 D59 G91 N93 D95
BS06 N25 B V163 L164 A165 H166 H201 E202 H205 H211 V81 L82 A83 H84 H119 E120 H123 H129 MOAD: ic50=18.4nM
PDBbind-CN: -logKd/Ki=7.74,IC50=18.4nM
BindingDB: IC50=18nM,Ki=18nM
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:1bqo, PDBe:1bqo, PDBj:1bqo
PDBsum1bqo
PubMed9733482
UniProtP08254|MMP3_HUMAN Stromelysin-1 (Gene Name=MMP3)

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