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4O6F

Structural Basis of Estrogen Receptor Alpha Methylation Mediated by Histone Methyltransferase SmyD2

Functional Information from GO Data
ChainGOidnamespacecontents
A0000122biological_processnegative regulation of transcription by RNA polymerase II
A0000993molecular_functionRNA polymerase II complex binding
A0002039molecular_functionp53 binding
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006325biological_processchromatin organization
A0006338biological_processchromatin remodeling
A0007507biological_processheart development
A0008168molecular_functionmethyltransferase activity
A0008285biological_processnegative regulation of cell population proliferation
A0016278molecular_functionlysine N-methyltransferase activity
A0016279molecular_functionprotein-lysine N-methyltransferase activity
A0018026biological_processpeptidyl-lysine monomethylation
A0018027biological_processpeptidyl-lysine dimethylation
A0032259biological_processmethylation
A0042054molecular_functionhistone methyltransferase activity
A0043516biological_processregulation of DNA damage response, signal transduction by p53 class mediator
A0046872molecular_functionmetal ion binding
A0046975molecular_functionhistone H3K36 methyltransferase activity
A0140938molecular_functionhistone H3 methyltransferase activity
A0140999molecular_functionhistone H3K4 trimethyltransferase activity
A1901796biological_processregulation of signal transduction by p53 class mediator
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 501
ChainResidue
ACYS52
ACYS55
ACYS74
ACYS78

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 502
ChainResidue
ACYS65
ACYS68
AHIS86
ACYS90

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 503
ChainResidue
ACYS262
ACYS264
ACYS267
ACYS209

site_idAC4
Number of Residues12
DetailsBINDING SITE FOR RESIDUE SAH A 504
ChainResidue
AGLY16
ALYS17
AARG19
AHIS137
AASN182
AALA203
AASN206
AHIS207
ATYR240
ATYR258
APHE260
AHOH615

site_idAC5
Number of Residues9
DetailsBINDING SITE FOR RESIDUE PE8 A 505
ChainResidue
AGLU190
ALYS309
ATYR344
AGLY348
ALEU351
ATRP356
ALYS387
AHOH661
BARG269

site_idAC6
Number of Residues1
DetailsBINDING SITE FOR RESIDUE NI A 506
ChainResidue
ACYS13

site_idAC7
Number of Residues2
DetailsBINDING SITE FOR RESIDUE NI A 507
ChainResidue
ACYS210
AHOH665

Functional Information from PROSITE/UniProt
site_idPS01360
Number of Residues40
DetailsZF_MYND_1 Zinc finger MYND-type signature. Hcey.Cftrkeglsk........CgrCkqafYCnveCqkedwpm..Hkle.C
ChainResidueDetails
AHIS51-CYS90

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues38
DetailsZN_FING: MYND-type => ECO:0000255|PROSITE-ProRule:PRU00134
ChainResidueDetails
ACYS52-CYS90

site_idSWS_FT_FI2
Number of Residues3
DetailsBINDING:
ChainResidueDetails
ALYS17
AASN206
ATYR258

site_idSWS_FT_FI3
Number of Residues8
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00134
ChainResidueDetails
ACYS52
ACYS55
ACYS65
ACYS68
ACYS74
ACYS78
AHIS86
ACYS90

site_idSWS_FT_FI4
Number of Residues1
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00190, ECO:0000269|PubMed:21724641
ChainResidueDetails
AHIS137

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER283

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PDB entries from 2024-07-24

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