Structure of PDB 5dxa Chain B

Receptor sequence

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

SVFSERTEESSAVQYFQFYGYLSQQQNMMQDYVRTGTYQRAILQNHTDFK
DKIVLDVGCGSGILSFFAAQAGARKIYAVEASTMAQHAEVLVKSNNLTDR
IVVIPGKVEEVSLPEQVDIIISEPMGYMLFNERMLESYLHAKKYLKPSGN
MFPTIGDVHLAPFTDEQLYMEQFTKANFWYQPSFHGVDLSALRGAAVDEY
FRQPVVDTFDIRILMAKSVKYTVNFLEAKEGDLHRIEIPFKFHMLHSGLV
HGLAFWFDVAFIGSIMTVWLSTAPTEPLTHWYQVRCLFQSPLFAKAGDTL
SGTCLLIANKRQSYDISIVAQVDQTGSKSSNLLDLKNPFFRYT

3D structure

PDB

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

Chain

Resolution

2.07 Å

3D
structure

Catalytic site residues are labeled in the structure
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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	Y149 F152 Y153 N161 E257 M259 Y261 E266 L412 T413 H414 W415 Y416 F474 Y476	Y15 F18 Y19 N27 E123 M125 Y127 E132 L278 T279 H280 W281 Y282 F340 Y342
BS02	SFG	B	Y149 F150 Y153 M162 R168 G192 C193 I197 L198 E214 A215 K241 E243 E257 M268	Y15 F16 Y19 M28 R34 G58 C59 I63 L64 E80 A81 K107 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:5dxa, PDBe:5dxa, PDBj:5dxa
PDBsum	5dxa
PubMed	26551522
UniProt	Q86X55\|CARM1_HUMAN Histone-arginine methyltransferase CARM1 (Gene Name=CARM1)

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