Structure of PDB 4h3x Chain B

Receptor sequence
>4h3xB (length=164) Species: 9606 (Homo sapiens) [Search protein sequence]
GFQTFEGDLKWHHHNITYWIQNYSEDLPRAVIDDAFARAFALWSAVTPLT
FTRVYSRDADIVIQFGVAEHGDGYPFDGKDGLLAHAFPPGPGIQGDAHFD
DDELWSLGKGVGYSLFLVAAHEFGHALGLDHSSVPEALMYPMYRFTEGPP
LHKDDVNGIRHLYG
3D structure
PDB4h3x Crystallization of bi-functional ligand protein complexes.
ChainB
Resolution1.764 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H226 E227 H230 H236
Catalytic site (residue number reindexed from 1) H121 E122 H125 H131
Enzyme Commision number 3.4.24.35: gelatinase B.
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 10B B Y245 P246 Y140 P141 BindingDB: IC50=200nM
BS02 ZN B H226 H230 H236 H121 H125 H131
BS03 ZN B H175 D177 H190 H203 H70 D72 H85 H98
BS04 CA B D182 G183 D185 L187 D205 E208 D77 G78 D80 L82 D100 E103
BS05 CA B D131 D206 E208 D26 D101 E103
BS06 CA B D165 G197 Q199 D201 D60 G92 Q94 D96
BS07 10B B L187 A189 L222 H226 E227 H230 H236 L243 Y245 M247 Y248 L82 A84 L117 H121 E122 H125 H131 L138 Y140 M142 Y143 BindingDB: IC50=200nM
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:4h3x, PDBe:4h3x, PDBj:4h3x
PDBsum4h3x
PubMed23567804
UniProtP14780|MMP9_HUMAN Matrix metalloproteinase-9 (Gene Name=MMP9)

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