Structure of PDB 5ztn Chain B

Receptor sequence
>5ztnB (length=397) Species: 9606 (Homo sapiens) [Search protein sequence]
GVDLGTENLYFQSMGKVKATPMTPEQAMKQYMQKLTAFEHHEIFSYPEIY
FLGLNAKKRQGMTGGPNNGGYDDDQGSYVQVPHDHVAYRYEVLKVIGKGS
FGQVVKAYDHKVHQHVALKMVRNEKRFHRQAAEEIRILEHLRKQDKDNTM
NVIHMLENFTFRNHICMTFELLSMNLYELIKKNKFQGFSLPLVRKFAHSI
LQCLDALHKNRIIHCDLKPENILLKQQGRSGIKVIDFGSSCYEHQRVYTY
IQSRFYRAPEVILGARYGMPIDMWSLGCILAELLTGYPLLPGEDEGDQLA
CMIELLGMPSQKLLDASKRAKNFVSSKGYPRYCTVTVLNGGRSRRGKLRG
PPESREWGNALKGCDDPLFLDFLKQCLEWDPAVRMTPGQALRHPWLR
3D structure
PDB5ztn Ancient drug curcumin impedes 26S proteasome activity by direct inhibition of dual-specificity tyrosine-regulated kinase 2.
ChainB
Resolution2.496 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) D216 K218 N221 D236 S253
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 CUR B F160 A176 K178 E193 I212 F228 L230 L231 S232 L282 I294 D295 F101 A117 K119 E134 I153 F169 L171 L172 S173 L223 I235 D236 MOAD: ic50=5nM
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:5ztn, PDBe:5ztn, PDBj:5ztn
PDBsum5ztn
PubMed29987021
UniProtQ92630|DYRK2_HUMAN Dual specificity tyrosine-phosphorylation-regulated kinase 2 (Gene Name=DYRK2)

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