6W6D

Crystal Structure of Human Protein arginine N-methyltransferase 6 (PRMT6) in complex with SGC6870 inhibitor

Functional Information from GO Data

Chain	GOid	namespace	contents
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	0006284	biological_process	base-excision repair
A	0006325	biological_process	chromatin organization
A	0006338	biological_process	chromatin remodeling
A	0006355	biological_process	regulation of DNA-templated transcription
A	0006974	biological_process	DNA damage response
A	0008168	molecular_function	methyltransferase activity
A	0008469	molecular_function	obsolete 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	0033554	biological_process	cellular response to stress
A	0035241	molecular_function	protein-arginine omega-N monomethyltransferase activity
A	0035242	molecular_function	protein-arginine omega-N asymmetric methyltransferase activity
A	0042054	molecular_function	histone methyltransferase activity
A	0042393	molecular_function	histone binding
A	0044020	molecular_function	histone H4R3 methyltransferase activity
A	0045652	biological_process	regulation of megakaryocyte differentiation
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	0090068	biological_process	positive regulation of cell cycle process
A	0140938	molecular_function	histone H3 methyltransferase activity
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 401

Chain	Residue
A	ARG66
A	PRO139
A	VAL140
A	GLU141
A	GLU155
A	MET166
A	SER169
A	HOH534
A	HOH569
A	HOH592
A	GLY90
A	ALA91
A	GLY92
A	THR93
A	LEU96
A	GLU112
A	ALA113
A	SER114

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site_id	AC2
Number of Residues	10
Details	binding site for residue T9A A 402

Chain	Residue
A	TRP156
A	GLY158
A	TYR159
A	GLY160
A	HIS163
A	GLU164
A	LEU256
A	PHE292
A	LEU343
A	PRO345

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	Active site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	1
Details	Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI3
Number of Residues	4
Details	Binding site: {}

Chain

Residue

Details

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