Structure of PDB 4aze Chain C

Receptor sequence
>4azeC (length=350) Species: 9606 (Homo sapiens) [Search protein sequence]
ERKVYNDGYDDDNYDYIVKNGEKWMDRYEIDSLIGKGSFGQVVKAYDRVE
QEWVAIKIIKNKKAFLNQAQIEVRLLELMNKHDTEMKYYIVHLKRHFMFR
NHLCLVFEMLSYNLYDLLRNTNFRGVSLNLTRKFAQQMCTALLFLATPEL
SIIHCDLKPENILLCNPKRSAIKIVDFGSSCQLGQRIYQYIQSRFYRSPE
VLLGMPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVEVLGIPP
AHILDQAPKARKFFEKLPDGTWNLKKTKDGKREYKPPGTRKLHNILGVET
GGPGGRRAGESGHTVADYLKFKDLILRMLDYDPKTRIQPYYALQHSFFKK
3D structure
PDB4aze Selectivity, Co-Crystal Structures and Neuroprotective Properties of Leucettines, a Family of Protein Kinase Inhibitors Derived from the Marine Sponge Alkaloid Leucettamine B.
ChainC
Resolution3.15 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) D156 K158 N161 D176 S193
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 3RA C I165 F170 A186 K188 F238 L241 L294 D307 I34 F39 A55 K57 F107 L110 L163 D176 BindingDB: IC50=7.6nM
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:4aze, PDBe:4aze, PDBj:4aze
PDBsum4aze
PubMed22998443
UniProtQ13627|DYR1A_HUMAN Dual specificity tyrosine-phosphorylation-regulated kinase 1A (Gene Name=DYRK1A)

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