Structure of PDB 6s1i Chain D

Receptor sequence
>6s1iD (length=346) Species: 9606 (Homo sapiens) [Search protein sequence]
VYNDGYDDDNYDYIVKNGEKWMDRYEIDSLIGKGSFGQVVKAYDRVEQEW
VAIKIIKNKKAFLNQAQIEVRLLELMNKHDTEMKYYIVHLKRHFMFRNHL
CLVFEMLSYNLYDLLRNTNFRGVSLNLTRKFAQQMCTALLFLATPELSII
HCDLKPENILLCNPKRSAIKIVDFGSSCQLGQIYQYIQSRFYRSPEVLLG
MPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVEVLGIPPAHIL
DQAPKARKFFEKLPDGTWNLKKTKDGKREYKPPGTRKLHNILGVETGGPG
GRRAGESGHTVADYLKFKDLILRMLDYDPKTRIQPYYALQHSFFKK
3D structure
PDB6s1i Mining Public Domain Data to Develop Selective DYRK1A Inhibitors.
ChainD
Resolution2.38 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) D287 K289 N292 D307 S324
Catalytic site (residue number reindexed from 1) D153 K155 N158 D173 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 KR8 D F170 V173 A186 K188 F238 M240 L241 L294 V306 D307 F36 V39 A52 K54 F104 M106 L107 L160 V172 D173 BindingDB: IC50=186nM
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:6s1i, PDBe:6s1i, PDBj:6s1i
PDBsum6s1i
PubMed32832032
UniProtQ13627|DYR1A_HUMAN Dual specificity tyrosine-phosphorylation-regulated kinase 1A (Gene Name=DYRK1A)

[Back to BioLiP]