Structure of PDB 4c04 Chain A Binding Site BS01

Receptor Information
>4c04 Chain A (length=327) Species: 10090 (Mus musculus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
QLYYECYSDVSVHEEMIADQVRTEAYRLGILKNWAALRGKTVLDVGAGTG
ILSIFCAQAGARRVYAVEASAIWQQAREVVRLNGLEDRVHVLPGPVETVE
LPERVDAIVSEWMGYGLLHESMLSSVLHARTKWLKEGGLLLPASAELFVA
PISDQMLEWRLGFWSQVKQHYGVDMSCMESFATRCLMGHSEIVVQDLSGE
DVLARPQRFAQLELARAGLEQELEAGVGGRFRCSCYGSAPLHGFAVWFQV
TFPGGKPLVLSTSPLHPATHWKQALLYLNEPVPVEQDTDISGEITLLPSP
DNPRRLRILLRYKVGDHEEKTKDFAME
Ligand information
Ligand IDSFG
InChIInChI=1S/C15H23N7O5/c16-6(1-2-7(17)15(25)26)3-8-10(23)11(24)14(27-8)22-5-21-9-12(18)19-4-20-13(9)22/h4-8,10-11,14,23-24H,1-3,16-17H2,(H,25,26)(H2,18,19,20)/t6-,7-,8+,10+,11+,14+/m0/s1
InChIKeyLMXOHSDXUQEUSF-YECHIGJVSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.7.0c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)C[C@H](CC[C@@H](C(=O)O)N)N)O)O)N
OpenEye OEToolkits 1.7.0c1nc(c2c(n1)n(cn2)C3C(C(C(O3)CC(CCC(C(=O)O)N)N)O)O)N
CACTVS 3.370N[CH](CC[CH](N)C(O)=O)C[CH]1O[CH]([CH](O)[CH]1O)n2cnc3c(N)ncnc23
CACTVS 3.370N[C@@H](CC[C@H](N)C(O)=O)C[C@H]1O[C@H]([C@H](O)[C@@H]1O)n2cnc3c(N)ncnc23
ACDLabs 12.01O=C(O)C(N)CCC(N)CC3OC(n2cnc1c(ncnc12)N)C(O)C3O
FormulaC15 H23 N7 O5
NameSINEFUNGIN;
ADENOSYL-ORNITHINE
ChEMBLCHEMBL1214186
DrugBankDB01910
ZINCZINC000004217451
PDB chain4c04 Chain A Residue 1377 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB4c04 Functional Insights from High Resolution Structures of Mouse Protein Arginine Methyltransferase 6.
Resolution1.576 Å
Binding residue
(original residue number in PDB)		M63 R69 G93 A94 G95 L99 E115 A116 E158 M169 S172
Binding residue
(residue number reindexed from 1)		M16 R22 G46 A47 G48 L52 E68 A69 E111 M122 S125
Annotation score3
Enzymatic activity
Catalytic site (original residue number in PDB) D66 E158 E167 H320
Catalytic site (residue number reindexed from 1) D19 E111 E120 H270
Enzyme Commision number 2.1.1.319: type I protein arginine methyltransferase.
Gene Ontology
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
Biological Process
GO:0000122 negative regulation of transcription by RNA polymerase II
GO:0006281 DNA 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: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

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:4c04, PDBe:4c04, PDBj:4c04
PDBsum4c04
PubMed26094878
UniProtQ6NZB1|ANM6_MOUSE Protein arginine N-methyltransferase 6 (Gene Name=Prmt6)

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