Structure of PDB 1biw Chain B

Receptor sequence
>1biwB (length=173) Species: 9606 (Homo sapiens) [Search protein sequence]
FRTFPGIPKWRKTHLTYRIVNYTPDLPKDAVDSAVEKALKVWEEVTPLTF
SRLYEGEADIMISFAVREHGDFYPFDGPGNVLAHAYAPGPGINGDAHFDD
DEQWTKDTTGTNLFLVAAHEIGHSLGLFHSANTEALMYPLYHSLTDLTRF
RLSQDDINGIQSLYGPPPDSPET
3D structure
PDB1biw Design and synthesis of conformationally-constrained MMP inhibitors.
ChainB
Resolution2.5 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 S80 B N162 V163 L164 V198 H201 E202 H205 H211 P221 L222 Y223 N80 V81 L82 V116 H119 E120 H123 H129 P139 L140 Y141 MOAD: ic50=104nM
PDBbind-CN: -logKd/Ki=6.98,IC50=104nM
BindingDB: IC50=104nM
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:1biw, PDBe:1biw, PDBj:1biw
PDBsum1biw
PubMed9873489
UniProtP08254|MMP3_HUMAN Stromelysin-1 (Gene Name=MMP3)

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