4HSG

Crystal structure of human PRMT3 in complex with an allosteric inhibitor (PRMT3- KTD)

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0016274	molecular_function	protein-arginine N-methyltransferase activity
A	0018216	biological_process	peptidyl-arginine methylation

Functional Information from PDB Data

site_id	AC1
Number of Residues	9
Details	BINDING SITE FOR RESIDUE KTD A 601

Chain	Residue
A	GLY245
A	GLU248
A	ASP389
A	LYS392
A	ARG396
A	VAL420
A	GLU422
A	THR466
A	ALA467

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	ACT_SITE: ACT_SITE => ECO:0000250|UniProtKB:O70467

Chain	Residue	Details
A	GLU346
A	GLU355

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site_id	SWS_FT_FI2
Number of Residues	6
Details	BINDING: BINDING => ECO:0000269|Ref.17, ECO:0007744|PDB:2FYT

Chain	Residue	Details
A	ARG256
A	GLY280
A	ASP302
A	ILE330
A	GLU331
A	SER360

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