Structure of PDB 5vd0 Chain A

Receptor sequence
>5vd0A (length=293) Species: 9606 (Homo sapiens) [Search protein sequence]
LGTENLYFLQPRRVSFRGEASETLQSPGYDPSRPESFFQQSFQRLSRLGH
GSYGEVFKVRSKEDGRLYAVKRSMSPFRGPKDRARKLAEVGSHEKVGQHP
CCVRLEQAWEEGGILYLQTELCGPSLQQHCEAWGASLPEAQVWGYLRDTL
LALAHLHSQGLVHLDVKPANIFLGPRGRCKLGDFGLLVELGTAGAGEVQE
GDPRYMAPELLQGSYGTAADVFSLGLTILEVACNMELPHGGEGWQQLRQG
YLPPEFTAGLSSELRSVLVMMLEPDPKLRATAEALLALPVLRQ
3D structure
PDB5vd0 Structural Basis of Wee Kinases Functionality and Inactivation by Diverse Small Molecule Inhibitors.
ChainA
Resolution2.13 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) D165 K167 N170 D183 D202
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 8X7 A L116 Y121 V124 K139 T187 C190 G191 P192 F240 L48 Y53 V56 K71 T119 C122 G123 P124 F172 MOAD: Kd=324nM
PDBbind-CN: -logKd/Ki=6.49,Kd=324nM
BindingDB: IC50=4940nM,Ki=470nM,Kd=324nM
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:5vd0, PDBe:5vd0, PDBj:5vd0
PDBsum5vd0
PubMed28792760
UniProtQ99640|PMYT1_HUMAN Membrane-associated tyrosine- and threonine-specific cdc2-inhibitory kinase (Gene Name=PKMYT1)

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