Structure of PDB 5uwn Chain D

Receptor sequence
>5uwnD (length=165) Species: 9606 (Homo sapiens) [Search protein sequence]
NVFPRTLKWSKMNLTYRIVNYTPDMTHSEVEKAFKKAFKVWSDVTPLNFT
RLHDGIADIMISFGIKEHGDFYPFDGPSGLLAHAFPPGPNYGGDAHFDDD
ETWTSSSKGYNLFLVAAHEFGHSLGLDHSKDPGALMFPIYTYTGKSHFML
PDDDVQGIQSLYGPG
3D structure
PDB5uwn Structure-Based Design and Synthesis of Potent and Selective Matrix Metalloproteinase 13 Inhibitors.
ChainD
Resolution3.2 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H222 E223 H226 H232
Catalytic site (residue number reindexed from 1) H118 E119 H122 H128
Enzyme Commision number 3.4.24.-
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 D H222 H226 H232 H118 H122 H128
BS02 ZN D H172 D174 H187 H200 H68 D70 H83 H96
BS03 CA D D179 G180 S182 L184 D202 E205 D75 G76 S78 L80 D98 E101
BS04 CA D D162 N194 G196 D198 D58 N90 G92 D94
BS05 8O7 D L184 L185 A186 L218 H222 E223 L239 F241 P242 I243 Y244 T245 T247 F252 L80 L81 A82 L114 H118 E119 L135 F137 P138 I139 Y140 T141 T143 F148 BindingDB: Ki=14nM,IC50=8.3nM
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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Biological Process
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Cellular Component
External links
PDB RCSB:5uwn, PDBe:5uwn, PDBj:5uwn
PDBsum5uwn
PubMed28653849
UniProtP45452|MMP13_HUMAN Collagenase 3 (Gene Name=MMP13)

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