Structure of PDB 5vcz Chain A

Receptor sequence
>5vczA (length=294) Species: 9606 (Homo sapiens) [Search protein sequence]
LGTENLYFQSQPRRVSFRGEASETLQSPGYDPSRPESFFQQSFQRLSRLG
HGSYGEVFKVRSKEDGRLYAVKRSMSPFRGPKDRARKLAEVGSHEKVGQH
PCCVRLEQAWEEGGILYLQTELCGPSLQQHCEAWGASLPEAQVWGYLRDT
LLALAHLHSQGLVHLDVKPANIFLGPRGRCKLGDFGLLVELGTAGAGEVQ
EGDPRYMAPELLQGSYGTAADVFSLGLTILEVACNMELPHGGEGWQQLRQ
GYLPPEFTAGLSSELRSVLVMMLEPDPKLRATAEALLALPVLRQ
3D structure
PDB5vcz Structural Basis of Wee Kinases Functionality and Inactivation by Diverse Small Molecule Inhibitors.
ChainA
Resolution1.5 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 XZN A L116 A137 K139 L185 T187 C190 G191 P192 Q196 F240 D251 L49 A70 K72 L118 T120 C123 G124 P125 Q129 F173 D184 MOAD: Kd=444nM
PDBbind-CN: -logKd/Ki=6.35,Kd=444nM
BindingDB: Kd=444nM
Gene Ontology
Molecular Function
GO:0004672 protein kinase activity
GO:0005524 ATP binding
Biological Process
GO:0006468 protein phosphorylation

View graph for
Molecular Function

View graph for
Biological Process
External links
PDB RCSB:5vcz, PDBe:5vcz, PDBj:5vcz
PDBsum5vcz
PubMed28792760
UniProtQ99640|PMYT1_HUMAN Membrane-associated tyrosine- and threonine-specific cdc2-inhibitory kinase (Gene Name=PKMYT1)

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