Structure of PDB 5vcy Chain A

Receptor sequence
>5vcyA (length=296) Species: 9606 (Homo sapiens) [Search protein sequence]
DLGTENLYFQLQPRRVSFRGEASETLQSPGYDPSRPESFFQQSFQRLSRL
GHGSYGEVFKVRSKEDGRLYAVKRSMSPFRGPKDRARKLAEVGSHEKVGQ
HPCCVRLEQAWEEGGILYLQTELCGPSLQQHCEAWGASLPEAQVWGYLRD
TLLALAHLHSQGLVHLDVKPANIFLGPRGRCKLGDFGLLVELGTAGAGEV
QEGDPRYMAPELLQGSYGTAADVFSLGLTILEVACNMELPHGGEGWQQLR
QGYLPPEFTAGLSSELRSVLVMMLEPDPKLRATAEALLALPVLRQP
3D structure
PDB5vcy Structural Basis of Wee Kinases Functionality and Inactivation by Diverse Small Molecule Inhibitors.
ChainA
Resolution1.56 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D233 K235 N238 D251 D270
Catalytic site (residue number reindexed from 1) D167 K169 N172 D185 D204
Enzyme Commision number 2.7.11.1: non-specific serine/threonine protein kinase.
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 DB8 A L116 A137 V138 K139 V171 L185 T187 C190 G191 P192 F240 L50 A71 V72 K73 V105 L119 T121 C124 G125 P126 F174 MOAD: Kd=270nM
PDBbind-CN: -logKd/Ki=6.57,Kd=270nM
BindingDB: Ki=13nM,IC50=704nM,Kd=350nM
Gene Ontology
Molecular Function
GO:0004672 protein kinase activity
GO:0005524 ATP binding
Biological Process
GO:0006468 protein phosphorylation

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Molecular Function
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Biological Process
External links
PDB RCSB:5vcy, PDBe:5vcy, PDBj:5vcy
PDBsum5vcy
PubMed28792760
UniProtQ99640|PMYT1_HUMAN Membrane-associated tyrosine- and threonine-specific cdc2-inhibitory kinase (Gene Name=PKMYT1)

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