Structure of PDB 7okp Chain D

Receptor sequence
>7okpD (length=344) Species: 10090 (Mus musculus) [Search protein sequence]
RSVFSERTEESSAVQYFQFYGYLSQQQNMMQDYVRTGTYQRAILQNHTDF
KDKIVLDVGCGSGILSFFAAQAGARKIYAVEASTMAQHAEVLVKSNNLTD
RIVVIPGKVEEVSLPEQVDIIISEPMGYMLFNERMLESYLHAKKYLKPSG
NMFPTIGDVHLAPFTDEQLYMEQFTKANFWYQPSFHGVDLSALRGAAVDE
YFRQPVVDTFDIRILMAKSVKYTVNFLEAKEGDLHRIEIPFKFHMLHSGL
VHGLAFWFDVAFIGSIMTVWLSTAPTEPLTHWYQVRCLFQSPLFAKAGDT
LSGTCLLIANKRQSYDISIVAQVDQTGSKSSNLLDLKNPFFRYT
3D structure
PDB7okp Structural Studies Provide New Insights into the Role of Lysine Acetylation on Substrate Recognition by CARM1 and Inform the Design of Potent Peptidomimetic Inhibitors.
ChainD
Resolution2.2 Å
3D
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
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 peptide D Q149 F153 Y154 Q159 N162 M163 D166 E258 Y262 N266 E267 H415 Y417 K471 P473 F475 Q15 F19 Y20 Q25 N28 M29 D32 E124 Y128 N132 E133 H281 Y283 K337 P339 F341
BS02 QVR D Y150 F151 Y154 G193 E215 E258 M269 Y16 F17 Y20 G59 E81 E124 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:7okp, PDBe:7okp, PDBj:7okp
PDBsum7okp
PubMed34569136
UniProtQ9WVG6|CARM1_MOUSE Histone-arginine methyltransferase CARM1 (Gene Name=Carm1)

[Back to BioLiP]