Structural Classification of Proteins
Family: Arginine methyltransferase
lacks the last two strands of the common fold replaced with a beta-sandwich oligomerisation subdomain
Lineage:
Root:
scop
Class:
Alpha and beta proteins (a/b)
[51349]
Mainly parallel beta sheets (beta-alpha-beta units)
Fold:
S-adenosyl-L-methionine-dependent methyltransferases
[53334]
core: 3 layers, a/b/a; mixed beta-sheet of 7 strands, order 3214576; strand 7 is antiparallel to the rest
Superfamily:
S-adenosyl-L-methionine-dependent methyltransferases
[53335]
uperfamily
Family:
Arginine methyltransferase
[53351]
lacks the last two strands of the common fold replaced with a beta-sandwich oligomerisation subdomain
Protein Domains:
Arginine methyltransferase, HMT1 [53352]
Baker's yeast (Saccharomyces cerevisiae)
[TaxId: 4932]
[53353] (1)
1g6q
mutant
chain 1
[34195]
chain 2
[34196]
chain 3
[34197]
chain 4
[34198]
chain 5
[34199]
chain 6
[34200]
Rat (Rattus norvegicus)
[TaxId: 10116]
[64116] (1)
1f3l
complexed with sah
chain a
[59630]
Protein arginine N-methyltransferase 1, PRMT1 [89749]
Rat (Rattus norvegicus)
[TaxId: 10116]
[89750] (3)
1ori
complexed with sah
chain a
[87339]
1orh
complexed with substrate peptide, chain B
complexed with gol, sah; mutant
chain a
[93455]
1or8
complexed with substrate peptide, chains B,C, D and E
complexed with gol, sah
chain a
[93451]
Protein arginine N-methyltransferase 3, PRMT3 [142581]
Human (Homo sapiens)
[TaxId: 9606]
[142582] (1)
SQ
O60678
221-531
2fyt
complexed with sah
region a:238-548
[134391]
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Generated from scop database 1.75 with scopm 1.101 on Wed Jun 3 10:42:06 2009
Copyright
© 1994-2009 The scop authors / scop@mrc-lmb.cam.ac.uk