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4C03

Crystal structure of M. musculus protein arginine methyltransferase PRMT6 reduced

Functional Information from GO Data
ChainGOidnamespacecontents
A0000122biological_processnegative regulation of transcription by RNA polymerase II
A0003682molecular_functionchromatin binding
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005730cellular_componentnucleolus
A0006281biological_processDNA repair
A0006325biological_processchromatin organization
A0006338biological_processchromatin remodeling
A0008168molecular_functionmethyltransferase activity
A0008469molecular_functionhistone arginine N-methyltransferase activity
A0010821biological_processregulation of mitochondrion organization
A0016274molecular_functionprotein-arginine N-methyltransferase activity
A0018216biological_processpeptidyl-arginine methylation
A0032259biological_processmethylation
A0035241molecular_functionprotein-arginine omega-N monomethyltransferase activity
A0035242molecular_functionprotein-arginine omega-N asymmetric methyltransferase activity
A0036211biological_processprotein modification process
A0042054molecular_functionhistone methyltransferase activity
A0042393molecular_functionhistone binding
A0044020molecular_functionhistone H4R3 methyltransferase activity
A0045892biological_processnegative regulation of DNA-templated transcription
A0070611molecular_functionhistone H3R2 methyltransferase activity
A0070612molecular_functionhistone H2AR3 methyltransferase activity
A0090398biological_processcellular senescence
A1901796biological_processregulation of signal transduction by p53 class mediator
A2000059biological_processnegative regulation of ubiquitin-dependent protein catabolic process
B0000122biological_processnegative regulation of transcription by RNA polymerase II
B0003682molecular_functionchromatin binding
B0005515molecular_functionprotein binding
B0005634cellular_componentnucleus
B0005654cellular_componentnucleoplasm
B0005730cellular_componentnucleolus
B0006281biological_processDNA repair
B0006325biological_processchromatin organization
B0006338biological_processchromatin remodeling
B0008168molecular_functionmethyltransferase activity
B0008469molecular_functionhistone arginine N-methyltransferase activity
B0010821biological_processregulation of mitochondrion organization
B0016274molecular_functionprotein-arginine N-methyltransferase activity
B0018216biological_processpeptidyl-arginine methylation
B0032259biological_processmethylation
B0035241molecular_functionprotein-arginine omega-N monomethyltransferase activity
B0035242molecular_functionprotein-arginine omega-N asymmetric methyltransferase activity
B0036211biological_processprotein modification process
B0042054molecular_functionhistone methyltransferase activity
B0042393molecular_functionhistone binding
B0044020molecular_functionhistone H4R3 methyltransferase activity
B0045892biological_processnegative regulation of DNA-templated transcription
B0070611molecular_functionhistone H3R2 methyltransferase activity
B0070612molecular_functionhistone H2AR3 methyltransferase activity
B0090398biological_processcellular senescence
B1901796biological_processregulation of signal transduction by p53 class mediator
B2000059biological_processnegative regulation of ubiquitin-dependent protein catabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues23
DetailsBINDING SITE FOR RESIDUE SFG A 1378
ChainResidue
ATYR50
AGLU115
AALA116
AGLY141
APRO142
AVAL143
AGLU144
AGLU158
AMET169
ASER172
AHOH2011
ATYR51
AHOH2058
AHOH2059
AHOH2139
AHOH2160
ATYR54
AMET63
AARG69
AGLY93
AALA94
AGLY95
ALEU99

site_idAC2
Number of Residues23
DetailsBINDING SITE FOR RESIDUE SFG B 1378
ChainResidue
BTYR50
BTYR51
BTYR54
BMET63
BARG69
BGLY93
BALA94
BGLY95
BLEU99
BGLU115
BALA116
BGLY141
BPRO142
BVAL143
BGLU144
BGLU158
BMET169
BSER172
BHOH2006
BHOH2009
BHOH2047
BHOH2048
BHOH2133

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: ACT_SITE => ECO:0000250
ChainResidueDetails
AGLU158
AGLU167
BGLU158
BGLU167

site_idSWS_FT_FI2
Number of Residues10
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AHIS60
BGLU144
AARG69
AGLY93
AGLU115
AGLU144
BHIS60
BARG69
BGLY93
BGLU115

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Asymmetric dimethylarginine; by autocatalysis => ECO:0000250
ChainResidueDetails
AARG38
BARG38

219140

PDB entries from 2024-05-01

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