Structure of PDB 8hlt Chain B

Receptor sequence
>8hltB (length=387) Species: 9606 (Homo sapiens) [Search protein sequence]
ATPMTPEQAMKQYMQKLTAFEHHEIFSYPEIYFLGLNAKKRQGMTGGPNN
GGYDDDQGSYVQVPHDHVAYRYEVLKVIGKGSFGQVVKAYDHKVHQHVAL
KMVRNEKRFHRQAAEEIRILEHLRKQDKDNTMNVIHMLENFTFRNHICMT
FELLSMNLYELIKKNKFQGFSLPLVRKFAHSILQCLDALHKNRIIHCDLK
PENILLKQQGRSGIKVIDFGSSCYEHQRVYTYIQSRFYRAPEVILGARYG
MPIDMWSLGCILAELLTGYPLLPGEDEGDQLACMIELLGMPSQKLLDASK
RAKNFVSSKGYPRYCTVTTLSDGSVVLNGGRSRRGKLRGPPESREWGNAL
KGCDDPLFLDFLKQCLEWDPAVRMTPGQALRHPWLRR
3D structure
PDB8hlt Discovery of Potent DYRK2 Inhibitors with High Selectivity, Great Solubility, and Excellent Safety Properties for the Treatment of Prostate Cancer.
ChainB
Resolution2.8 Å
3D
structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
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 XSE B I155 F160 V163 A176 F228 E229 L231 S232 M233 N234 E237 L282 I294 D295 I78 F83 V86 A99 F151 E152 L154 S155 M156 N157 E160 L205 I217 D218
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:8hlt, PDBe:8hlt, PDBj:8hlt
PDBsum8hlt
PubMed36800260
UniProtQ92630|DYRK2_HUMAN Dual specificity tyrosine-phosphorylation-regulated kinase 2 (Gene Name=DYRK2)

[Back to BioLiP]