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4Y2H

Crystal structure of human protein arginine methyltransferase PRMT6 bound to SAH and an aryl pyrazole inhibitor

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
A0006284biological_processbase-excision repair
A0006325biological_processchromatin organization
A0006338biological_processchromatin remodeling
A0008168molecular_functionmethyltransferase activity
A0008170molecular_functionN-methyltransferase 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
A0045652biological_processregulation of megakaryocyte differentiation
A0045892biological_processnegative regulation of DNA-templated transcription
A0070611molecular_functionhistone H3R2 methyltransferase activity
A0070612molecular_functionhistone H2AR3 methyltransferase activity
A0090398biological_processcellular senescence
A0140938molecular_functionhistone H3 methyltransferase activity
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
B0006284biological_processbase-excision repair
B0006325biological_processchromatin organization
B0006338biological_processchromatin remodeling
B0008168molecular_functionmethyltransferase activity
B0008170molecular_functionN-methyltransferase 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
B0045652biological_processregulation of megakaryocyte differentiation
B0045892biological_processnegative regulation of DNA-templated transcription
B0070611molecular_functionhistone H3R2 methyltransferase activity
B0070612molecular_functionhistone H2AR3 methyltransferase activity
B0090398biological_processcellular senescence
B0140938molecular_functionhistone H3 methyltransferase activity
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 Residues22
Detailsbinding site for residue SAH A 401
ChainResidue
ATYR47
ALEU96
AGLU112
AALA113
APRO139
AVAL140
AGLU141
AMET166
ASER169
A49K402
AHOH554
ATYR48
AHOH555
AHOH561
AHOH638
ATYR51
AMET60
AARG66
AGLY90
AALA91
AGLY92
AILE95

site_idAC2
Number of Residues10
Detailsbinding site for residue 49K A 402
ChainResidue
ATYR51
AVAL56
AGLU59
AGLU155
AMET157
ATYR159
AGLU164
AHIS317
ASAH401
AHOH564

site_idAC3
Number of Residues23
Detailsbinding site for residue SAH B 401
ChainResidue
BTYR47
BTYR51
BMET60
BARG66
BGLY90
BALA91
BILE95
BLEU96
BGLU112
BALA113
BSER114
BPRO139
BVAL140
BGLU141
BGLU155
BMET166
BSER169
B49K402
BHOH524
BHOH527
BHOH530
BHOH536
BHOH553

site_idAC4
Number of Residues11
Detailsbinding site for residue 49K B 402
ChainResidue
BTYR51
BVAL56
BGLU59
BGLU155
BMET157
BTYR159
BGLU164
BHIS317
BTRP318
BSAH401
BHOH575

site_idAC5
Number of Residues9
Detailsbinding site for residue GOL B 403
ChainResidue
BLEU162
BSER165
BLEU344
BPRO350
BARG351
BARG352
BLEU353
BHOH556
BHOH577

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: ACT_SITE => ECO:0000250
ChainResidueDetails
AGLU155
AGLU164
BGLU155
BGLU164

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AHIS57
BHIS57

site_idSWS_FT_FI3
Number of Residues8
DetailsBINDING:
ChainResidueDetails
AARG66
AGLY90
AGLU112
AGLU141
BARG66
BGLY90
BGLU112
BGLU141

site_idSWS_FT_FI4
Number of Residues6
DetailsMOD_RES: Asymmetric dimethylarginine; by autocatalysis => ECO:0000269|PubMed:23866860
ChainResidueDetails
AARG29
AARG35
AARG37
BARG29
BARG35
BARG37

223166

PDB entries from 2024-07-31

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