Structure of PDB 5ue3 Chain A

Receptor sequence
>5ue3A (length=228) Species: 9606 (Homo sapiens) [Search protein sequence]
DRQLAEEYLYRYGYTRVAEMRGESKSLGPALLLLQKQLSLPETGELDSAT
LKAMRTPRCGVPDLGRFQTFEGDLKWHHHNITYWIQNYSEDLPRAVIDDA
FARAFALWSAVTPLTFTRVYSRDADIVIQFGVAEHGDGYPFDGKDGLLAH
AFPPGPGIQGDAHFDDDELWSLGKGQGYSLFLVAAHEFGHALGLDHSSVP
EALMYPMYRFTEGPPLHKDDVNGIRHLY
3D structure
PDB5ue3 Discovery of a highly selective chemical inhibitor of matrix metalloproteinase-9 (MMP-9) that allosterically inhibits zymogen activation.
ChainA
Resolution1.599 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) H186 E187 H190 H196
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 C59 H186 H190 H196
BS02 ZN A H175 D177 H190 H203 H135 D137 H150 H163
BS03 CA A D182 G183 D185 L187 D205 E208 D142 G143 D145 L147 D165 E168
BS04 CA A S129 E130 D206 S89 E90 D166
BS05 CA A D165 G197 Q199 D201 D125 G157 Q159 D161
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:5ue3, PDBe:5ue3, PDBj:5ue3
PDBsum5ue3
PubMed28860188
UniProtP14780|MMP9_HUMAN Matrix metalloproteinase-9 (Gene Name=MMP9)

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