Structure of PDB 5ue4 Chain A

Receptor sequence
>5ue4A (length=227) Species: 9606 (Homo sapiens) [Search protein sequence]
TDRQLAEEYLYRYGYTRVAEMRGESLGPALLLLQKQLSLPETGELDSATL
KAMRTPRCGVPDLGRFQTFEGDLKWHHHNITYWIQNYSEDLPRAVIDDAF
ARAFALWSAVTPLTFTRVYSRDADIVIQFGVAEHGDGYPFDGKDGLLAHA
FPPGPGIQGDAHFDDDELWSLGKGQGYSLFLVAAHEFGHALGLDHSSVPE
ALMYPMYRFTEGPPLHKDDVNGIRHLY
3D structure
PDB5ue4 Discovery of a highly selective chemical inhibitor of matrix metalloproteinase-9 (MMP-9) that allosterically inhibits zymogen activation.
ChainA
Resolution1.8 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) H185 E186 H189 H195
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 ZN A C99 H226 H230 H236 C58 H185 H189 H195
BS02 ZN A H175 D177 H190 H203 H134 D136 H149 H162
BS03 CA A D182 G183 D185 L187 D205 E208 D141 G142 D144 L146 D164 E167
BS04 CA A D165 G197 Q199 D201 D124 G156 Q158 D160
BS05 CA A D131 D206 E208 D90 D165 E167
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:5ue4, PDBe:5ue4, PDBj:5ue4
PDBsum5ue4
PubMed28860188
UniProtP14780|MMP9_HUMAN Matrix metalloproteinase-9 (Gene Name=MMP9)

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