Structure of PDB 5a3x Chain B

Receptor sequence
>5a3xB (length=341) Species: 9606 (Homo sapiens) [Search protein sequence]
RKVYNDGYDDDNYDYIVKNGEKWMDRYEIDSLIGKGSFGQVVKAYDRVEQ
EWVAIKIIKNKKAFLNQAQIEVRLLELMNKHDTEMKYYIVHLKRHFMFRN
HLCLVFEMLSYNLYDLLRNTNFRGVSLNLTRKFAQQMCTALLFLATPELS
IIHCDLKPENILLCNPKRSAIKIVDFGSSCQLGQRIYQYIQSRFYRSPEV
LLGMPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVEVLGIPPA
HILDQAPKARKFFEKLPDGTWNLKYKPPGTRKLHNILGVETGGPGGRRAG
ESGHTVADYLKFKDLILRMLDYDPKTRIQPYYALQHSFFKK
3D structure
PDB5a3x Probing the ATP-Binding Pocket of Protein Kinase Dyrk1A with Benzothiazole Fragment Molecules
ChainB
Resolution2.26 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D287 K289 N292 D307 S324
Catalytic site (residue number reindexed from 1) D155 K157 N160 D175 S192
Enzyme Commision number 2.7.11.23: [RNA-polymerase]-subunit kinase.
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 QIV B F170 A186 K188 L241 L294 D307 F38 A54 K56 L109 L162 D175 MOAD: ic50=0.8uM
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
GO:0046777 protein autophosphorylation

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Molecular Function
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Biological Process
External links
PDB RCSB:5a3x, PDBe:5a3x, PDBj:5a3x
PDBsum5a3x
PubMed27736065
UniProtQ13627|DYR1A_HUMAN Dual specificity tyrosine-phosphorylation-regulated kinase 1A (Gene Name=DYRK1A)

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