Structure of PDB 3wst Chain J

Receptor sequence
>3wstJ (length=644) Species: 6239 (Caenorhabditis elegans) [Search protein sequence]
MFLEKINQKTGEREWVVAEEDYDMAQELARSRFGDMILDFDRNDKFLAGL
KTTIAEKKHENTDGKVHVLDIGTGTGLLSLMAAREGADKVTALEVFKPMG
DCARHITSNSPWSDKITVISERSTDVSQIGGSRADIIVAEVFDTELIGEG
ALRTFKEALERLAKPGCRVVPSTGNVYIVPVESHLLKMFNDIPRLNGEKD
EEPLGRCSGTAAVFDVQLSEMKTHEFRELSEPIVAFKFDFEHEEKIIFDE
SFVREAVAHSSGTIDALLMWWDIDMDRNGTTFIDMGPKWKNKNNYAWRDH
WMQAVYYLPEKKKVEMNQTFEIVCNHDEFSLWFSNVGKDKSRSYCVCGLH
SMLSRQTVYHVNEMFENQKFKDEVDKLSKGLHVATVGEGSFLGLLAAKTA
KRVTIIDGNERFRDIFFKYIHYYKLTNVEIIEKVTSLTDSPDIVLAEPFY
MSAMNPWNHLRFLYDVEVLKMMHGDELRVEPHMGVLKAIPEKFEDLQNIA
SDVGTVNGFDLSFFDEISTKARTATDAIVDEQSLWEYAGIVKGDAVEILR
FPIDGRVSSQKCVVNIDNMSSSNAIPMWMEWEFGGINLSTGLLSISSAGV
PEWNKGYKQGVYFPITALRNDKSLCLHALFDKSTGDINFQFGKS
3D structure
PDB3wst Protein arginine methyltransferase 7 has a novel homodimer-like structure formed by tandem repeats
ChainJ
Resolution2.39 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) E140 E149
Catalytic site (residue number reindexed from 1) E140 E149
Enzyme Commision number 2.1.1.-
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 SAH J R42 G72 T73 L78 E94 V95 R122 S123 E140 V141 T154 R42 G72 T73 L78 E94 V95 R122 S123 E140 V141 T154
Gene Ontology
Molecular Function
GO:0008168 methyltransferase activity
GO:0016274 protein-arginine N-methyltransferase activity
GO:0042054 histone methyltransferase activity
Biological Process
GO:0006338 chromatin remodeling
GO:0006479 protein methylation
GO:0018216 peptidyl-arginine methylation
GO:0032259 methylation

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Molecular Function
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Biological Process
External links
PDB RCSB:3wst, PDBe:3wst, PDBj:3wst
PDBsum3wst
PubMed24726727
UniProtQ9XW42|ANM7_CAEEL Protein arginine N-methyltransferase 7 (Gene Name=prmt-7)

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