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

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	Active site: {"evidences":[{"source":"UniProtKB","id":"O70467","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	6
Details	Binding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAR-2006","submissionDatabase":"PDB data bank","title":"The crystal structure of human HMT1 HNRNP methyltransferase-like 3 in complex with SAH.","authoringGroup":["Structural genomics consortium (SGC)"]}},{"source":"PDB","id":"2FYT","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---