Structure of PDB 3kvw Chain A

Receptor sequence
>3kvwA (length=406) Species: 9606 (Homo sapiens) [Search protein sequence]
HHSSGVDLGTENLYFQSMGKVKATPMTPEQAMKQYMQKLTAFEHHEIFSY
PEIYFLGLNAKKRQGMTGGPNNGGYDDDQGSYVQVPHDHVAYRYEVLKVI
GKGSFGQVVKAYDHKVHQHVALKMVRNEKRFHRQAAEEIRILEHLRKQDK
DNTMNVIHMLENFTFRNHICMTFELLSMNLYELIKKNKFQGFSLPLVRKF
AHSILQCLDALHKNRIIHCDLKPENILLKQQGRSGIKVIDFGSSCYEHQR
VYTYIQSRFYRAPEVILGARYGMPIDMWSLGCILAELLTGYPLLPGEDEG
DQLACMIELLGMPSQKLLDASKRAKNFVSSKGYPRYCTVTTLSDVVLNGG
RSRRGKLRGPPESREWGNALKGCDDPLFLDFLKQCLEWDPAVRMTPGQAL
RHPWLR
3D structure
PDB3kvw Crystal Structure of dual-specificity tyrosine phosphorylation regulated kinase 2 (DYRK2) in complex with an indirubin ligand
ChainA
Resolution2.28 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D275 K277 N280 D295 S312
Catalytic site (residue number reindexed from 1) D220 K222 N225 D240 S257
Enzyme Commision number 2.7.12.1: dual-specificity 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 IRB A I155 A176 K178 F228 L230 L231 S232 I294 D295 I100 A121 K123 F173 L175 L176 S177 I239 D240 PDBbind-CN: -logKd/Ki=6.89,IC50=0.13uM
Gene Ontology
Molecular Function
GO:0004672 protein kinase activity
GO:0004712 protein serine/threonine/tyrosine 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:3kvw, PDBe:3kvw, PDBj:3kvw
PDBsum3kvw
PubMed
UniProtQ92630|DYRK2_HUMAN Dual specificity tyrosine-phosphorylation-regulated kinase 2 (Gene Name=DYRK2)

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