Structure of PDB 5vd3 Chain A

Receptor sequence
>5vd3A (length=293) Species: 9606 (Homo sapiens) [Search protein sequence]
DLGTENLYFQQPRRVSFRGEASETLQSPGYDPSRPESFFQQSFQRLSRLG
HGSYGEVFKVRSKEDGRLYAVKRSMSPFRGPKDRARKLAEVGSHEKVGQH
PCCVRLEQAWEEGGILYLQTELCGPSLQQHCEAWGASLPEAQVWGYLRDT
LLALAHLHSQGLVHLDVKPANIFLGPRGRCKLGDFGLLVELGTAGAGEVQ
EGDPRYMAPELLQGSYGTAADVFSLGLTILEVACNMELPHGGEGWQQLRQ
GYLPPEFTAGLSSELRSVLVMMLEPDPKLRATAEALLALPVLR
3D structure
PDB5vd3 Structural Basis of Wee Kinases Functionality and Inactivation by Diverse Small Molecule Inhibitors.
ChainA
Resolution1.8 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) D166 K168 N171 D184 D203
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 H8H A L116 A137 K139 L185 T187 C190 G191 P192 F240 L49 A70 K72 L118 T120 C123 G124 P125 F173 MOAD: Kd=2817nM
PDBbind-CN: -logKd/Ki=5.55,Kd=2817nM
BindingDB: IC50=418nM,Ki=40nM,Kd=2817nM
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:5vd3, PDBe:5vd3, PDBj:5vd3
PDBsum5vd3
PubMed28792760
UniProtQ99640|PMYT1_HUMAN Membrane-associated tyrosine- and threonine-specific cdc2-inhibitory kinase (Gene Name=PKMYT1)

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