Structure of PDB 4c4a Chain A Binding Site BS02

Receptor Information
>4c4a Chain A (length=641) Species: 10090 (Mus musculus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
HQEIARSSYADMLHDKDRNIKYYQGIRAAVSRVKDRGQKALVLDIGTGTG
LLSMMAVTAGADFCYAIEVFKPMAEAAVKIVERNGFSDKIKVINKHSTEV
TVGPDGDLPCRANILITELFDTELIGEGALPSYEHAHKHLVQEDCEAVPH
RATVYAQLVESRRMWSWNKLFPVRVRTSLGEQVIVPPSELERCPGAPSVC
DIQLNQVSPADFTVLSDVLPMFSVDFSKQVSSSAACHSRQFVPLASGQAQ
VVLSWWDIEMDPEGKIKCTMAPFWAQTDPQELQWRDHWMQCVYFLPQEEP
VVQGSPRCLVAHHDDYCVWYSLQRTSPQVRPVCDCQAHLLWNRPRFGEIN
DQDRTDHYAQALRTVLLPGSVCLCVSDGSLLSMLAHHLGAEQVFTVESSV
ASYRLMKRIFKVNHLEDKISVINKRPELLTAADLEGKKVSLLLGEPFFTT
SLLPWHNLYFWYVRTSVDQHLAPGAVVMPQAASLHAVIVEFRDLWRIRSP
CGDCEGFDVHIMDDMIKHSLDFRESREAEPHPLWEYPCRSLSKPQEILTF
DFQQPIPQQPMQSKGTMELTRPGKSHGAVLWMEYQLTPDSTISTGLINPG
DCCWNPHCKQAVYFLSTPRSVSYVVEFHPLTGDITMEFRLA
Ligand information
Ligand IDDMX
InChIInChI=1S/C12H19NO3S/c1-13(2,9-6-10-17(14,15)16)11-12-7-4-3-5-8-12/h3-5,7-8H,6,9-11H2,1-2H3
InChIKeyMEJASPJNLSQOAG-UHFFFAOYSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0C[N+](C)(CCCS(=O)(=O)[O-])Cc1ccccc1
ACDLabs 10.04[O-]S(=O)(=O)CCC[N+](C)(Cc1ccccc1)C
CACTVS 3.341C[N+](C)(CCC[S]([O-])(=O)=O)Cc1ccccc1
FormulaC12 H19 N O3 S
Name3-[BENZYL(DIMETHYL)AMMONIO]PROPANE-1-SULFONATE
ChEMBL
DrugBank
ZINC
PDB chain4c4a Chain A Residue 2690 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB4c4a Structural Insight Into Arginine Methylation by the Mouse Protein Arginine Methyltransferase 7: A Zinc Finger Freezes the Mimic of the Dimeric State Into a Single Active Site.
Resolution1.7 Å
Binding residue
(original residue number in PDB)		Y492 Y495 P676 G679
Binding residue
(residue number reindexed from 1)		Y459 Y462 P629 G632
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) D41 E144 E153 H313
Catalytic site (residue number reindexed from 1) D15 E118 E127 H287
Enzyme Commision number 2.1.1.321: type III protein arginine methyltransferase.
Gene Ontology
Molecular Function
GO:0005515 protein binding
GO:0008168 methyltransferase activity
GO:0008757 S-adenosylmethionine-dependent methyltransferase activity
GO:0016274 protein-arginine N-methyltransferase activity
GO:0035241 protein-arginine omega-N monomethyltransferase activity
GO:0035243 protein-arginine omega-N symmetric methyltransferase activity
GO:0042393 histone binding
GO:0043021 ribonucleoprotein complex binding
GO:0044020 histone H4R3 methyltransferase activity
GO:0140939 histone H4 methyltransferase activity
Biological Process
GO:0000387 spliceosomal snRNP assembly
GO:0006325 chromatin organization
GO:0006479 protein methylation
GO:0018216 peptidyl-arginine methylation
GO:0030154 cell differentiation
GO:0032259 methylation
GO:0071514 genomic imprinting
Cellular Component
GO:0001650 fibrillar center
GO:0005634 nucleus
GO:0005654 nucleoplasm
GO:0005737 cytoplasm
GO:0005829 cytosol

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:4c4a, PDBe:4c4a, PDBj:4c4a
PDBsum4c4a
PubMed25195753
UniProtQ922X9|ANM7_MOUSE Protein arginine N-methyltransferase 7 (Gene Name=Prmt7)

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