Structure of PDB 5dx0 Chain B

Receptor sequence

>5dx0B (length=343) Species: 9606 (Homo sapiens) [Search protein sequence]

SVFSERTEESSAVQYFQFYGYLSQQQNMMQDYVRTGTYQRAILQNHTDFK
DKIVLDVGCGSGILSFFAAQAGARKIYAVEASTMAQHAEVLVKSNNLTDR
IVVIPGKVEEVSLPEQVDIIISEPMGYMLFNERMLESYLHAKKYLKPSGN
MFPTIGDVHLAPFTDEQLYMEQFTKANFWYQPSFHGVDLSALRGAAVDEY
FRQPVVDTFDIRILMAKSVKYTVNFLEAKEGDLHRIEIPFKFHMLHSGLV
HGLAFWFDVAFIGSIMTVWLSTAPTEPLTHWYQVRCLFQSPLFAKAGDTL
SGTCLLIANKRQSYDISIVAQVDQTGSKSSNLLDLKNPFFRYT

3D structure

PDB

5dx0 Structural Insights into Ternary Complex Formation of Human CARM1 with Various Substrates.

Chain

Resolution

2.05 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)	D165 E257 E266 H414
Catalytic site (residue number reindexed from 1)	D31 E123 E132 H280
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	B	Q148 F152 Y153 N161 D165 E257 M259 Y261 N265 E266 H414 Y416	Q14 F18 Y19 N27 D31 E123 M125 Y127 N131 E132 H280 Y282
BS02	SFG	B	Y149 F150 Y153 Q159 M162 R168 G192 C193 I197 L198 E214 A215 K241 V242 E243 E257 M268	Y15 F16 Y19 Q25 M28 R34 G58 C59 I63 L64 E80 A81 K107 V108 E109 E123 M134

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:5dx0, PDBe:5dx0, PDBj:5dx0
PDBsum	5dx0
PubMed	26551522
UniProt	Q86X55\|CARM1_HUMAN Histone-arginine methyltransferase CARM1 (Gene Name=CARM1)

[Back to BioLiP]