Structure of PDB 5lxd Chain B

Receptor sequence
>5lxdB (length=386) Species: 9606 (Homo sapiens) [Search protein sequence]
PMTPEQAMKQYMQKLTAFEHHEIFSYPEIYFLGLNAKKRQGMTGGPNNGG
YDDDQGSYVQVPHDHVAYRYEVLKVIGKGSFGQVVKAYDHKVHQHVALKM
VRNEKRFHRQAAEEIRILEHLRKQDKDNTMNVIHMLENFTFRNHICMTFE
LLSMNLYELIKKNKFQGFSLPLVRKFAHSILQCLDALHKNRIIHCDLKPE
NILLKQQGRSGIKVIDFGSSCYEHQRVYTYIQSRFYRAPEVILGARYGMP
IDMWSLGCILAELLTGYPLLPGEDEGDQLACMIELLGMPSQKLLDASKRA
KNFVSSKGYPRYCTVTTLSDGSVVLNGGRSRRGKLRGPPESREWGNALKG
CDDPLFLDFLKQCLEWDPAVRMTPGQALRHPWLRRR
3D structure
PDB5lxd An Unusual Binding Model of the Methyl 9-Anilinothiazolo[5,4-f] quinazoline-2-carbimidates (EHT 1610 and EHT 5372) Confers High Selectivity for Dual-Specificity Tyrosine Phosphorylation-Regulated Kinases.
ChainB
Resolution2.58 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) D196 K198 N201 D216 S233
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 7A7 B G156 V163 F228 L231 L282 I294 D295 G77 V84 F149 L152 L203 I215 D216
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

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:5lxd, PDBe:5lxd, PDBj:5lxd
PDBsum5lxd
PubMed27766861
UniProtQ92630|DYRK2_HUMAN Dual specificity tyrosine-phosphorylation-regulated kinase 2 (Gene Name=DYRK2)

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