Structure of PDB 5a54 Chain B Binding Site BS01

Receptor Information
>5a54 Chain B (length=340) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
RKVYNDGYDDDNYDYIVKNGEKWMDRYEIDSLIGKGSFGQVVKAYDRVEQ
EWVAIKIIKNKKAFLNQAQIEVRLLELMNKHDTEMKYYIVHLKRHFMFRN
HLCLVFEMLSYNLYDLLRNTNFRGVSLNLTRKFAQQMCTALLFLATPELS
IIHCDLKPENILLCNPKRSAIKIVDFGSSCQLGQRIYQYIQSRFYRSPEV
LLGMPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVEVLGIPPA
HILDQAPKARKFFEKLPDGTWNLKYKPPGTRKLHNILGVETGGPGGRRAG
ESGHTVADYLKFKDLILRMLDYDPKTRIQPYYALQHSFFK
Ligand information
Ligand ID5PW
InChIInChI=1S/C9H7N3O3S/c1-5(13)10-9-11-7-3-2-6(12(14)15)4-8(7)16-9/h2-4H,1H3,(H,10,11,13)
InChIKeyXARDSBCDZPSYTN-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.385CC(=O)Nc1sc2cc(ccc2n1)[N+]([O-])=O
OpenEye OEToolkits 1.7.6CC(=O)Nc1nc2ccc(cc2s1)[N+](=O)[O-]
FormulaC9 H7 N3 O3 S
NameN-(6-nitro-1,3-benzothiazol-2-yl)ethanamide
ChEMBLCHEMBL1213041
DrugBank
ZINCZINC000005495244
PDB chain5a54 Chain B Residue 1482 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB5a54 Probing the ATP-Binding Pocket of Protein Kinase Dyrk1A with Benzothiazole Fragment Molecules
Resolution2.63 Å
Binding residue
(original residue number in PDB)		I165 A186 F238 L241 L294
Binding residue
(residue number reindexed from 1)		I33 A54 F106 L109 L162
Annotation score1
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.
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

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:5a54, PDBe:5a54, PDBj:5a54
PDBsum5a54
PubMed27736065
UniProtQ13627|DYR1A_HUMAN Dual specificity tyrosine-phosphorylation-regulated kinase 1A (Gene Name=DYRK1A)

[Back to BioLiP]