Structure of PDB 4mq1 Chain C

Receptor sequence
>4mq1C (length=329) Species: 9606 (Homo sapiens) [Search protein sequence]
VYNDGYDDDNYDYIVKNGEKWMDRYEIDSLIGKGSFGQVVKAYDRVEQEW
VAIKIIKNKKAFLNQAQIEVRLLELMNKHMKYYIVHLKRHFMFRNHLCLV
FEMLSYNLYDLLRNTNFRGVSLNLTRKFAQQMCTALLFLATPELSIIHCD
LKPENILLCNPKRSAIKIVDFGSSCQLGQRIYQYIQSRFYRSPEVLLGMP
YDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVEVLGIPPAHILDQ
APKARKFFEKLPDGTWNLKKTKDGKREYKPPGTRKLHNILGVETTVADYL
KFKDLILRMLDYDPKTRIQPYYALQHSFF
3D structure
PDB4mq1 Pyrido[2,3-d]pyrimidines: Discovery and preliminary SAR of a novel series of DYRK1B and DYRK1A inhibitors.
ChainC
Resolution2.35 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) D150 K152 N155 D170 S187
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 2C3 C I165 K167 G168 G171 V173 K188 F238 M240 L241 S242 Y243 N292 L294 V306 D307 I31 K33 G34 G37 V39 K54 F101 M103 L104 S105 Y106 N155 L157 V169 D170 BindingDB: IC50=12nM
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:4mq1, PDBe:4mq1, PDBj:4mq1
PDBsum4mq1
PubMed24239188
UniProtQ13627|DYR1A_HUMAN Dual specificity tyrosine-phosphorylation-regulated kinase 1A (Gene Name=DYRK1A)

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