Structure of PDB 4nct Chain B

Receptor sequence
>4nctB (length=334) Species: 9606 (Homo sapiens) [Search protein sequence]
RKVYNDGYDDDNYDYIVKNGEKWMDRYEIDSLIGKGSFGQVVKAYDRVEQ
EWVAIKIIKNKKAFLNQAQIEVRLLELMNKYYIVHLKRHFMFRNHLCLVF
EMLSYNLYDLLRNTNFRGVSLNLTRKFAQQMCTALLFLATPELSIIHCDL
KPENILLCNPKRSAIKIVDFGSSCQLGQRIYQYIQSRFYRSPEVLLGMPY
DLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVEVLGIPPAHILDQA
PKARKFFEKLPDGTWNLKYKPPGTRKLHNILGVETGGPGGRRAGESGHTV
ADYLKFKDLILRMLDYDPKTRIQPYYALQHSFFK
3D structure
PDB4nct The structure of a dual-specificity tyrosine phosphorylation-regulated kinase 1A-PKC412 complex reveals disulfide-bridge formation with the anomalous catalytic loop HRD(HCD) cysteine.
ChainB
Resolution2.597 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) D149 K151 N154 D169 S186
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 2K2 B I165 V173 A186 K188 L241 E291 L294 D307 I33 V41 A54 K56 L103 E153 L156 D169 BindingDB: Kd=100nM
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:4nct, PDBe:4nct, PDBj:4nct
PDBsum4nct
PubMed25945585
UniProtQ13627|DYR1A_HUMAN Dual specificity tyrosine-phosphorylation-regulated kinase 1A (Gene Name=DYRK1A)

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