Structure of PDB 5uwn Chain A

Receptor sequence
>5uwnA (length=161) Species: 9606 (Homo sapiens) [Search protein sequence]
RTLKWSKMNLTYRIVNYTPDMTHSEVEKAFKKAFKVWSDVTPLNFTRLHD
GIADIMISFGIKEHGDFYPFDGPSGLLAHAFPPGPNYGGDAHFDDDETWT
SSSKGYNLFLVAAHEFGHSLGLDHSKDPGALMFPIYTYTGKSHFMLPDDD
VQGIQSLYGPG
3D structure
PDB5uwn Structure-Based Design and Synthesis of Potent and Selective Matrix Metalloproteinase 13 Inhibitors.
ChainA
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) H114 E115 H118 H124
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 A H222 H226 H232 H114 H118 H124
BS02 ZN A H172 D174 H187 H200 H64 D66 H79 H92
BS03 CA A D179 G180 S182 L184 D202 E205 D71 G72 S74 L76 D94 E97
BS04 CA A D162 N194 G196 D198 D54 N86 G88 D90
BS05 8O7 A L184 L185 L218 H222 E223 F241 P242 I243 Y244 T245 T247 P255 L76 L77 L110 H114 E115 F133 P134 I135 Y136 T137 T139 P147 PDBbind-CN: -logKd/Ki=7.87,Ki=13.5nM
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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Molecular Function
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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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