Structure of PDB 6ogn Chain A

Receptor sequence
>6ognA (length=617) Species: 10090 (Mus musculus) [Search protein sequence]
SYADMLHDKDRNIKYYQGIRAAVSRVKDRGQKALVLDIGTGTGLLSMMAV
TAGADFCYAIEVFKPMAEAAVKIVERNGFSDKIKVINKHSTEVTVGPDGD
LPCRANILITELFDTELIGEGALPSYEHAHKHLVQEDCEAVPHRATVYAQ
LVESRRMWSWNKLFPVRVRTSLGEQVIVPPSELERCPGAPSVCDIQLNQV
SPADFTVLSDVLPMFSVDFSKQVSSSAACHSRQFVPLASGQAQVVLSWWD
IEMDPEGKIKCTMAPFWAQTDPQELQWRDMQCVYFLPQEEPVVQGSPRCL
VAHHDDYCVWYSLQRTSPQVRPVCDCQAHLLWNRPRFGEINDQDRTDHYA
QALRTVLLPGSVCLCVSDGSLLSMLAHHLGAEQVFTVESSVASYRLMKRI
FKVNHLEDKISVINKRPELLTAADLEGKKVSLLLGEPFFTTSLLPWHNLY
FWYVRTSVDQHLAPGAVVMPQAASLHAVIVEFRDLWRIRSPCGDCEGFDV
HIMDSREAEPHPLWEYPCRSLSKPQEILTFDFQQPIPQQPMQSKGTMELT
RPGKSHGAVLWMEYQLTPDSTISTGLINDCCWNPHCKQAVYFLSRSVSYV
VEFHPLTGDITMEFRLA
3D structure
PDB6ogn Pharmacological inhibition of PRMT7 links arginine monomethylation to the cellular stress response.
ChainA
Resolution2.4 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D41 E144 E153
Catalytic site (residue number reindexed from 1) D8 E111 E120
Enzyme Commision number 2.1.1.321: type III protein arginine methyltransferase.
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 ZN A C219 C366 C368 H371 C186 C324 C326 H329
BS02 MJ7 A Y35 R44 I71 G72 E94 V95 H122 S123 L145 F146 W282 Y2 R11 I38 G39 E61 V62 H89 S90 L112 F113 W249
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

View graph for
Molecular Function

View graph for
Biological Process

View graph for
Cellular Component
External links
PDB RCSB:6ogn, PDBe:6ogn, PDBj:6ogn
PDBsum6ogn
PubMed32409666
UniProtQ922X9|ANM7_MOUSE Protein arginine N-methyltransferase 7 (Gene Name=Prmt7)

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