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6N3G

Crystal structure of histone lysine methyltransferase SmyD2 in complex with polyethylene glycol

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 Residues16
Detailsbinding site for residue SAH A 501
ChainResidue
AGLY16
AASN206
AHIS207
ATYR240
ATYR258
APHE260
AHOH602
AHOH624
ALYS17
AARG19
AGLU135
AHIS137
ALYS162
ACYS181
AASN182
AALA203

site_idAC2
Number of Residues11
Detailsbinding site for residue 12P A 502
ChainResidue
AGLU190
ALYS309
AHIS310
ATYR344
AGLY348
ALEU351
ATYR352
ATRP356
ALYS387
AARG390
AGLY394

site_idAC3
Number of Residues2
Detailsbinding site for residue NI A 503
ChainResidue
AEOH505
AEOH507

site_idAC4
Number of Residues7
Detailsbinding site for residue EOH A 505
ChainResidue
APHE184
AVAL202
AALA203
AMET205
ATHR238
ATYR240
ANI503

site_idAC5
Number of Residues3
Detailsbinding site for residue EOH A 506
ChainResidue
APRO15
ALYS17
AGLU263

site_idAC6
Number of Residues4
Detailsbinding site for residue EOH A 507
ChainResidue
ATHR185
ATYR240
ANI503
AHOH650

site_idAC7
Number of Residues1
Detailsbinding site for residue EOH A 508
ChainResidue
AARG67

site_idAC8
Number of Residues3
Detailsbinding site for residue EOH A 509
ChainResidue
AASP188
AGLU190
ASER192

site_idAC9
Number of Residues4
Detailsbinding site for residue ZN A 510
ChainResidue
ACYS52
ACYS55
ACYS74
ACYS78

site_idAD1
Number of Residues4
Detailsbinding site for residue ZN A 511
ChainResidue
ACYS65
ACYS68
AHIS86
ACYS90

site_idAD2
Number of Residues4
Detailsbinding site for residue ZN A 512
ChainResidue
ACYS209
ACYS262
ACYS264
ACYS267

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
ACYS74
ACYS78
AHIS86
ACYS90
ACYS52
ACYS55
ACYS65
ACYS68

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 2024-05-15

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