Structure of PDB 5isg Chain B

Receptor sequence
>5isgB (length=343) Species: 10090 (Mus musculus) [Search protein sequence]
RSVFSERTEESSAVQYFQFYGYLSQQQNMMQDYVRTGTYQRAILQNHTDF
KDKIVLDVGCGSGILSFFAAQAGARKIYAVEASTMAQHAEVLVKSNNLTD
RIVVIPGKVEEVSLPEQVDIIISEPMGYMLFNERMLESYLHAKKYLKPSG
NMFPTIGDVHLAPFTDEQLYMEQFTKANFWYQPSFHGVDLSALRGAAVDE
YFRQPVVDTFDIRILMAKSVKYTVNFLEAKEGDLHRIEIPFKFHMLHSGL
VHGLAFWFDVAFIGSIMTVWLSTAPTEPLTHWYQVRCLFQSPLFAKAGDT
LSGTCLLIANKRQSYDISIVAQVDQTGSKSSNLLDLKNPFFRY
3D structure
PDB5isg Crystal structure of mouse CARM1 in complex with inhibitor SA0707
ChainB
Resolution2.418 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) D166 E258 E267 H415
Catalytic site (residue number reindexed from 1) D32 E124 E133 H281
Enzyme Commision number 2.1.1.319: type I 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 6D6 B Y150 F151 Y154 R169 G193 C194 S196 E215 A216 K242 V243 E244 E258 M260 M269 Y16 F17 Y20 R35 G59 C60 S62 E81 A82 K108 V109 E110 E124 M126 M135
Gene Ontology
Molecular Function
GO:0016274 protein-arginine N-methyltransferase activity
Biological Process
GO:0018216 peptidyl-arginine methylation

View graph for
Molecular Function

View graph for
Biological Process
External links
PDB RCSB:5isg, PDBe:5isg, PDBj:5isg
PDBsum5isg
PubMed
UniProtQ9WVG6|CARM1_MOUSE Histone-arginine methyltransferase CARM1 (Gene Name=Carm1)

[Back to BioLiP]