Structure of PDB 5ue3 Chain B

Receptor sequence
>5ue3B (length=221) Species: 9606 (Homo sapiens) [Search protein sequence]
DRQLAEEYLYRYGYTRVAEGPALLLLQKQLSLPETGELDSATLKAMRTPR
CGVPDLGRFQTFEGDLKWHHHNITYWIQNYSEDLPRAVIDDAFARAFALW
SAVTPLTFTRVYSRDADIVIQFGVAEHGDGYPFDGKDGLLAHAFPPGPGI
QGDAHFDDDELWSLGKGQGYSLFLVAAHEFGHALGLDHSSVPEALMYPMY
RFTEGPPLHKDDVNGIRHLYG
3D structure
PDB5ue3 Discovery of a highly selective chemical inhibitor of matrix metalloproteinase-9 (MMP-9) that allosterically inhibits zymogen activation.
ChainB
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) H178 E179 H182 H188
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 B C99 H226 H230 H236 C51 H178 H182 H188
BS02 ZN B H175 D177 H190 H203 H127 D129 H142 H155
BS03 CA B D182 G183 D185 L187 D205 E208 D134 G135 D137 L139 D157 E160
BS04 CA B D165 G197 Q199 D201 D117 G149 Q151 D153
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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