5FQN

Crystal structure of M. musculus protein arginine methyltransferase PRMT6 with SAH at 1.65 Angstroms

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000122	biological_process	negative regulation of transcription by RNA polymerase II
A	0003682	molecular_function	chromatin binding
A	0005515	molecular_function	protein binding
A	0005634	cellular_component	nucleus
A	0005654	cellular_component	nucleoplasm
A	0005730	cellular_component	nucleolus
A	0006281	biological_process	DNA repair
A	0006325	biological_process	chromatin organization
A	0006338	biological_process	chromatin remodeling
A	0006974	biological_process	DNA damage response
A	0008168	molecular_function	methyltransferase activity
A	0008469	molecular_function	histone arginine N-methyltransferase activity
A	0010821	biological_process	regulation of mitochondrion organization
A	0016274	molecular_function	protein-arginine N-methyltransferase activity
A	0016740	molecular_function	transferase activity
A	0018216	biological_process	peptidyl-arginine methylation
A	0032259	biological_process	methylation
A	0035241	molecular_function	protein-arginine omega-N monomethyltransferase activity
A	0035242	molecular_function	protein-arginine omega-N asymmetric methyltransferase activity
A	0036211	biological_process	protein modification process
A	0042054	molecular_function	histone methyltransferase activity
A	0042393	molecular_function	histone binding
A	0044020	molecular_function	histone H4R3 methyltransferase activity
A	0045892	biological_process	negative regulation of DNA-templated transcription
A	0070611	molecular_function	histone H3R2 methyltransferase activity
A	0070612	molecular_function	histone H2AR3 methyltransferase activity
A	0090398	biological_process	cellular senescence
A	1901796	biological_process	regulation of signal transduction by p53 class mediator
A	2000059	biological_process	negative regulation of ubiquitin-dependent protein catabolic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	18
Details	BINDING SITE FOR RESIDUE SAH A 1378

Chain	Residue
A	ARG69
A	PRO142
A	VAL143
A	GLU144
A	GLU158
A	MET169
A	SER172
A	HOH2024
A	HOH2025
A	HOH2071
A	GLY93
A	ALA94
A	GLY95
A	LEU99
A	GLU115
A	ALA116
A	SER117
A	GLY141

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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

Chain	Residue	Details
A	GLU158
A	GLU167

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site_id	SWS_FT_FI2
Number of Residues	5
Details	BINDING: BINDING => ECO:0000250

Chain	Residue	Details
A	HIS60
A	ARG69
A	GLY93
A	GLU115
A	GLU144

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site_id	SWS_FT_FI3
Number of Residues	1
Details	MOD_RES: Asymmetric dimethylarginine; by autocatalysis => ECO:0000250

Chain	Residue	Details
A	ARG38

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