Structure of PDB 4mq2 Chain A

Receptor sequence
>4mq2A (length=344) Species: 9606 (Homo sapiens) [Search protein sequence]
YNDGYDDDNYDYIVKNGEKWMDRYEIDSLIGKGSFGQVVKAYDRVEQEWV
AIKIIKNKKAFLNQAQIEVRLLELMNKHDTEMKYYIVHLKRHFMFRNHLC
LVFEMLSYNLYDLLRNTNFRGVSLNLTRKFAQQMCTALLFLATPELSIIH
CDLKPENILLCNPKRSAIKIVDFGSSCQLGQRIYQYIQSRFYRSPEVLLG
MPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVEVLGIPPAHIL
DQAPKARKFFEKLPDGTWNLKKTKKREYKPPGTRKLHNILGVETGGPGGR
RAGESGHTVADYLKFKDLILRMLDYDPKTRIQPYYALQHSFFKK
3D structure
PDB4mq2 Pyrido[2,3-d]pyrimidines: Discovery and preliminary SAR of a novel series of DYRK1B and DYRK1A inhibitors.
ChainA
Resolution2.8 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) D152 K154 N157 D172 S189
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 2C4 A F170 K188 F238 M240 L241 S242 Y243 L294 V306 D307 F35 K53 F103 M105 L106 S107 Y108 L159 V171 D172 PDBbind-CN: -logKd/Ki=7.01,IC50=0.097uM
BindingDB: IC50=97nM
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
View graph for
Biological Process
External links
PDB RCSB:4mq2, PDBe:4mq2, PDBj:4mq2
PDBsum4mq2
PubMed24239188
UniProtQ13627|DYR1A_HUMAN Dual specificity tyrosine-phosphorylation-regulated kinase 1A (Gene Name=DYRK1A)

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