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Receptor Information

>4qqk Chain A (length=324) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]

ECYSDVSVHEEMIADRVRTDAYRLGILRNWAALRGKTVLDVGAGTGILSI
FCAQAGARRVYAVEASAIWQQAREVVRFNGLEDRVHVLPGPVETVELPEQ
VDAIVSEWMGYGLLHESMLSSVLHARTKWLKEGGLLLPASAELFIVPISD
QMLEWRLGFWSQVKQHYGVDMSCLEGFATRCLMGHSEIVVQGLSGEDVLA
RPQRFAQLELSRAGLEQELEAGVGGRFRCSCYGSAPMHGFAIWFQVTFPG
GEKPLVLSTSPFHPATHWKQALLYLNEPVQVEQDTDVSGEITLLPSRDNP
RRLRVLLRYKVGDQEEKTKDFAME

Ligand ID

37H

InChI

InChI=1S/C17H27N9O5/c18-8(16(29)30)2-1-7(4-22-17(20)21)3-9-11(27)12(28)15(31-9)26-6-25-10-13(19)23-5-24-14(10)26/h5-9,11-12,15,27-28H,1-4,18H2,(H,29,30)(H2,19,23,24)(H4,20,21,22)/t7-,8-,9+,11+,12+,15+/m0/s1

InChIKey

PRQKNHVENSAKGM-TVDBPQCTSA-N

SMILES

Software	SMILES
ACDLabs 12.01	O=C(O)C(N)CCC(CNC(=[N@H])N)CC3OC(n2cnc1c(ncnc12)N)C(O)C3O
OpenEye OEToolkits 1.7.6	c1nc(c2c(n1)n(cn2)C3C(C(C(O3)CC(CCC(C(=O)O)N)CNC(=N)N)O)O)N
CACTVS 3.385	N[C@@H](CC[C@H](CNC(N)=N)C[C@H]1O[C@H]([C@H](O)[C@@H]1O)n2cnc3c(N)ncnc23)C(O)=O
OpenEye OEToolkits 1.7.6	[H]/N=C(/N)\NC[C@@H](CC[C@@H](C(=O)O)N)C[C@@H]1[C@H]([C@H]([C@@H](O1)n2cnc3c2ncnc3N)O)O
CACTVS 3.385	N[CH](CC[CH](CNC(N)=N)C[CH]1O[CH]([CH](O)[CH]1O)n2cnc3c(N)ncnc23)C(O)=O

Formula

C17 H27 N9 O5

Name

(5S)-5-{[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxytetrahydrofuran-2-yl]methyl}-N~6~-carbamimidoyl-L-lysine

PDB chain

4qqk Chain A Residue 401 [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	4qqk Structural basis of arginine asymmetrical dimethylation by PRMT6.
Resolution	1.88 Å
Binding residue (original residue number in PDB)	M60 R66 G90 A91 G92 L96 E112 A113 S114 P139 V140 E155 M166
Binding residue (residue number reindexed from 1)	M12 R18 G42 A43 G44 L48 E64 A65 S66 P91 V92 E107 M118
Annotation score	3

Catalytic site (original residue number in PDB)	D63 E155 E164 H317
Catalytic site (residue number reindexed from 1)	D15 E107 E116 H267
Enzyme Commision number	2.1.1.319: type I protein arginine methyltransferase.

	Molecular Function
GO:0003682	chromatin binding
GO:0005515	protein binding
GO:0008168	methyltransferase activity
GO:0008469	histone arginine N-methyltransferase activity
GO:0016274	protein-arginine N-methyltransferase activity
GO:0035241	protein-arginine omega-N monomethyltransferase activity
GO:0035242	protein-arginine omega-N asymmetric methyltransferase activity
GO:0042054	histone methyltransferase activity
GO:0042393	histone binding
GO:0044020	histone H4R3 methyltransferase activity
GO:0070611	histone H3R2 methyltransferase activity
GO:0070612	histone H2AR3 methyltransferase activity
GO:0140938	histone H3 methyltransferase activity

	Biological Process
GO:0000122	negative regulation of transcription by RNA polymerase II
GO:0006281	DNA repair
GO:0006284	base-excision repair
GO:0006325	chromatin organization
GO:0006338	chromatin remodeling
GO:0010821	regulation of mitochondrion organization
GO:0018216	peptidyl-arginine methylation
GO:0032259	methylation
GO:0036211	protein modification process
GO:0045652	regulation of megakaryocyte differentiation
GO:0045892	negative regulation of DNA-templated transcription
GO:0090398	cellular senescence
GO:1901796	regulation of signal transduction by p53 class mediator
GO:2000059	negative regulation of ubiquitin-dependent protein catabolic process

	Cellular Component
GO:0005634	nucleus
GO:0005654	nucleoplasm
GO:0005730	nucleolus

PDB	RCSB:4qqk, PDBe:4qqk, PDBj:4qqk
PDBsum	4qqk
PubMed	27480107
UniProt	Q96LA8\|ANM6_HUMAN Protein arginine N-methyltransferase 6 (Gene Name=PRMT6)

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Structure of PDB 4qqk Chain A Binding Site BS01