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6CBX

Crystal structure of human SET and MYND Domain Containing protein 2 with MTF1497

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
B0000122biological_processnegative regulation of transcription by RNA polymerase II
B0000993molecular_functionRNA polymerase II complex binding
B0002039molecular_functionp53 binding
B0005515molecular_functionprotein binding
B0005634cellular_componentnucleus
B0005654cellular_componentnucleoplasm
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006325biological_processchromatin organization
B0006338biological_processchromatin remodeling
B0007507biological_processheart development
B0008168molecular_functionmethyltransferase activity
B0008285biological_processnegative regulation of cell population proliferation
B0016278molecular_functionlysine N-methyltransferase activity
B0016279molecular_functionprotein-lysine N-methyltransferase activity
B0018026biological_processpeptidyl-lysine monomethylation
B0018027biological_processpeptidyl-lysine dimethylation
B0032259biological_processmethylation
B0042054molecular_functionhistone methyltransferase activity
B0043516biological_processregulation of DNA damage response, signal transduction by p53 class mediator
B0046872molecular_functionmetal ion binding
B0046975molecular_functionhistone H3K36 methyltransferase activity
B0140938molecular_functionhistone H3 methyltransferase activity
B0140999molecular_functionhistone H3K4 trimethyltransferase activity
B1901796biological_processregulation of signal transduction by p53 class mediator
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue ZN A 1001
ChainResidue
ACYS52
ACYS55
ACYS74
ACYS78

site_idAC2
Number of Residues4
Detailsbinding site for residue ZN A 1002
ChainResidue
ACYS65
ACYS68
AHIS86
ACYS90

site_idAC3
Number of Residues4
Detailsbinding site for residue ZN A 1003
ChainResidue
ACYS262
ACYS264
ACYS267
ACYS209

site_idAC4
Number of Residues17
Detailsbinding site for residue EW1 A 1004
ChainResidue
AGLY16
ALYS17
AGLU135
AHIS137
ACYS181
AASN182
AGLY183
APHE184
AALA203
AASN206
AHIS207
ATYR240
ATYR258
APHE260
AGLU263
AHOH1157
AHOH1214

site_idAC5
Number of Residues2
Detailsbinding site for residue CL A 1005
ChainResidue
AILE241
AASP242

site_idAC6
Number of Residues7
Detailsbinding site for residue EDO A 1006
ChainResidue
APRO37
AALA38
ALYS115
ATHR123
APRO124
ASER125
AHOH1166

site_idAC7
Number of Residues4
Detailsbinding site for residue EDO A 1007
ChainResidue
AASP242
ATYR245
ATYR370
ATYR374

site_idAC8
Number of Residues4
Detailsbinding site for residue ZN B 1001
ChainResidue
BCYS52
BCYS55
BCYS74
BCYS78

site_idAC9
Number of Residues4
Detailsbinding site for residue ZN B 1002
ChainResidue
BCYS65
BCYS68
BHIS86
BCYS90

site_idAD1
Number of Residues4
Detailsbinding site for residue ZN B 1003
ChainResidue
BCYS209
BCYS262
BCYS264
BCYS267

site_idAD2
Number of Residues17
Detailsbinding site for residue EW1 B 1004
ChainResidue
BGLY16
BLYS17
BGLU135
BHIS137
BCYS181
BASN182
BGLY183
BPHE184
BALA203
BASN206
BHIS207
BTYR240
BTYR258
BPHE260
BGLU263
BHOH1154
BHOH1185

site_idAD3
Number of Residues3
Detailsbinding site for residue CL B 1005
ChainResidue
BILE241
BASP242
BARG253

site_idAD4
Number of Residues5
Detailsbinding site for residue EDO B 1006
ChainResidue
ASER329
BARG67
BLYS87
BSER91
BHIS163

site_idAD5
Number of Residues4
Detailsbinding site for residue EDO B 1007
ChainResidue
AHIS157
BHIS158
BHOH1105
BHOH1153

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 Residues76
DetailsZN_FING: MYND-type => ECO:0000255|PROSITE-ProRule:PRU00134
ChainResidueDetails
ACYS52-CYS90
BCYS52-CYS90

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING:
ChainResidueDetails
ALYS17
AASN206
ATYR258
BLYS17
BASN206
BTYR258

site_idSWS_FT_FI3
Number of Residues16
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00134
ChainResidueDetails
ACYS52
BCYS55
BCYS65
BCYS68
BCYS74
BCYS78
BHIS86
BCYS90
ACYS55
ACYS65
ACYS68
ACYS74
ACYS78
AHIS86
ACYS90
BCYS52

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00190, ECO:0000269|PubMed:21724641
ChainResidueDetails
AHIS137
BHIS137

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER283
BSER283

219140

PDB entries from 2024-05-01

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