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Receptor Information

>4nct Chain B (length=334) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]

RKVYNDGYDDDNYDYIVKNGEKWMDRYEIDSLIGKGSFGQVVKAYDRVEQ
EWVAIKIIKNKKAFLNQAQIEVRLLELMNKYYIVHLKRHFMFRNHLCLVF
EMLSYNLYDLLRNTNFRGVSLNLTRKFAQQMCTALLFLATPELSIIHCDL
KPENILLCNPKRSAIKIVDFGSSCQLGQRIYQYIQSRFYRSPEVLLGMPY
DLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVEVLGIPPAHILDQA
PKARKFFEKLPDGTWNLKYKPPGTRKLHNILGVETGGPGGRRAGESGHTV
ADYLKFKDLILRMLDYDPKTRIQPYYALQHSFFK

Ligand ID

2K2

InChI

InChI=1S/C35H30N4O4/c1-35-32(42-3)25(37(2)34(41)19-11-5-4-6-12-19)17-26(43-35)38-23-15-9-7-13-20(23)28-29-22(18-36-33(29)40)27-21-14-8-10-16-24(21)39(35)31(27)30(28)38/h4-16,25-26,32H,17-18H2,1-3H3,(H,36,40)/t25-,26-,32-,35+/m1/s1

InChIKey

BMGQWWVMWDBQGC-IIFHNQTCSA-N

SMILES

Software	SMILES
ACDLabs 12.01	O=C(c1ccccc1)N(C9C(OC)C8(OC(n6c5c3n8c2ccccc2c3c4c(C(=O)NC4)c5c7ccccc67)C9)C)C
OpenEye OEToolkits 1.7.6	C[C@@]12[C@@H]([C@@H](C[C@@H](O1)n3c4ccccc4c5c3c6n2c7ccccc7c6c8c5C(=O)NC8)N(C)C(=O)c9ccccc9)OC
CACTVS 3.385	CO[C@@H]1[C@@H](C[C@H]2O[C@]1(C)n3c4ccccc4c5c6CNC(=O)c6c7c8ccccc8n2c7c35)N(C)C(=O)c9ccccc9
OpenEye OEToolkits 1.7.6	CC12C(C(CC(O1)n3c4ccccc4c5c3c6n2c7ccccc7c6c8c5C(=O)NC8)N(C)C(=O)c9ccccc9)OC
CACTVS 3.385	CO[CH]1[CH](C[CH]2O[C]1(C)n3c4ccccc4c5c6CNC(=O)c6c7c8ccccc8n2c7c35)N(C)C(=O)c9ccccc9

Formula

C35 H30 N4 O4

Name

PKC412;
N-[(5S,6R,7R,9R)-6-methoxy-5-methyl-14-oxo-6,7,8,9,15,16-hexahydro-5H,14H-5,9-epoxy-4b,9a,15-triazadibenzo[b,h]cyclonon a[1,2,3,4-jkl]cyclopenta[e]-as-indacen-7-yl]-N-methylbenzamide

PDB chain

4nct Chain B Residue 501 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]

Receptor-Ligand Complex Structure

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Structure summary

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PDB	4nct 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.
Resolution	2.597 Å
Binding residue (original residue number in PDB)	I165 V173 A186 K188 L241 E291 L294 D307
Binding residue (residue number reindexed from 1)	I33 V41 A54 K56 L103 E153 L156 D169
Annotation score	1
Binding affinity	BindingDB: Kd=100nM

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.

	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

PDB	RCSB:4nct, PDBe:4nct, PDBj:4nct
PDBsum	4nct
PubMed	25945585
UniProt	Q13627\|DYR1A_HUMAN Dual specificity tyrosine-phosphorylation-regulated kinase 1A (Gene Name=DYRK1A)

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Structure of PDB 4nct Chain B Binding Site BS01