Structure of PDB 3anr Chain D

Receptor sequence
>3anrD (length=341) Species: 9606 (Homo sapiens) [Search protein sequence]
KVYNDGYDDDNYDYIVKNGEKWMDRYEIDSLIGKGSFGQVVKAYDRVEQE
WVAIKIIKNKKAFLNQAQIEVRLLELMNKHDTEMKYYIVHLKRHFMFRNH
LCLVFEMLSYNLYDLLRNTNFRGVSLNLTRKFAQQMCTALLFLATPELSI
IHCDLKPENILLCNPKRSAIKIVDFGSSCQLGQRIYQYIQSRFYRSPEVL
LGMPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVEVLGIPPAH
ILDQAPKARKFFEKLPDGTWNLKKREYKPPGTRKLHNILGVETGGPGGRR
AGESGHTVADYLKFKDLILRMLDYDPKTRIQPYYALQHSFF
3D structure
PDB3anr Development of a novel selective inhibitor of the Down syndrome-related kinase Dyrk1A
ChainD
Resolution2.6 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) D154 K156 N159 D174 S191
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 HRM D F170 A186 K188 F238 L241 L294 V306 D307 F37 A53 K55 F105 L108 L161 V173 D174 BindingDB: IC50=80nM,Ki=33nM
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:3anr, PDBe:3anr, PDBj:3anr
PDBsum3anr
PubMed20981014
UniProtQ13627|DYR1A_HUMAN Dual specificity tyrosine-phosphorylation-regulated kinase 1A (Gene Name=DYRK1A)

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