Structure of PDB 7a5b Chain A

Receptor sequence
>7a5bA (length=340) Species: 9606 (Homo sapiens) [Search protein sequence]
YNDGYDDDNYDYIVKNGEKWMDRYEIDSLIGKGSFGQVVKAYDRVEQEWV
AIKIIKNKKAFLNQAQIEVRLLELMNKHDTEMKYYIVHLKRHFMFRNHLC
LVFEMLSYNLYDLLRNTNFRGVSLNLTRKFAQQMCTALLFLATPELSIIH
CDLKPENILLCNPKRSAIKIVDFGSSCQLGQRIYQYIQSRFYRSPEVLLG
MPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVEVLGIPPAHIL
DQAPKARKFFEKLPDGTWNLKKEYKPPGTRKLHNILGVETGGPGGRRAGE
SGHTVADYLKFKDLILRMLDYDPKTRIQPYYALQHSFFKK
3D structure
PDB7a5b Fragment-Derived Selective Inhibitors of Dual-Specificity Kinases DYRK1A and DYRK1B.
ChainA
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) 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 MFR A I165 A186 K188 F238 L241 L294 V306 D307 I30 A51 K53 F103 L106 L159 V171 D172
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:7a5b, PDBe:7a5b, PDBj:7a5b
PDBsum7a5b
PubMed34143631
UniProtQ13627|DYR1A_HUMAN Dual specificity tyrosine-phosphorylation-regulated kinase 1A (Gene Name=DYRK1A)

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