4X41

Crystal Structure of Protein Arginine Methyltransferase PRMT8

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
B	0016274	molecular_function	protein-arginine N-methyltransferase activity
B	0018216	biological_process	peptidyl-arginine methylation

Functional Information from PDB Data

site_id	AC1
Number of Residues	17
Details	binding site for residue SAH A 401

Chain	Residue
A	HIS86
A	GLU141
A	CYS142
A	GLY167
A	LYS168
A	VAL169
A	GLU185
A	MET196
A	THR199
A	ARG95
A	GLY119
A	SER120
A	GLY121
A	THR122
A	ILE124
A	LEU125
A	ILE140

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Functional Information from PROSITE/UniProt

site_id	PS00329
Number of Residues	14
Details	HSP70_2 Heat shock hsp70 proteins family signature 2. VLDVGSGTgilSMF

Chain	Residue	Details
A	VAL115-PHE128

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	ACT_SITE: ACT_SITE => ECO:0000250|UniProtKB:Q63009

Chain	Residue	Details
A	GLU194
A	ALA203
B	GLU194
B	ALA203

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site_id	SWS_FT_FI2
Number of Residues	2
Details	BINDING: BINDING => ECO:0000250|UniProtKB:Q63009

Chain	Residue	Details
A	ARG95
B	ARG95

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site_id	SWS_FT_FI3
Number of Residues	4
Details	BINDING: BINDING => ECO:0000305|PubMed:26529540, ECO:0000305|PubMed:26876602, ECO:0007744|PDB:4X41, ECO:0007744|PDB:5DST

Chain	Residue	Details
A	TYR104
A	GLN150
B	TYR104
B	GLN150

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site_id	SWS_FT_FI4
Number of Residues	4
Details	BINDING: BINDING => ECO:0000305|PubMed:26876602, ECO:0007744|PDB:5DST

Chain	Residue	Details
A	PHE128
A	VAL179
B	PHE128
B	VAL179

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site_id	SWS_FT_FI5
Number of Residues	2
Details	MOD_RES: Omega-N-methylarginine; by autocatalysis => ECO:0000269|PubMed:17925405

Chain	Residue	Details
A	PRO67
B	PRO67

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site_id	SWS_FT_FI6
Number of Residues	2
Details	MOD_RES: Asymmetric dimethylarginine; by autocatalysis => ECO:0000269|PubMed:17925405

Chain	Residue	Details
A	HIS82
B	HIS82

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