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3OXF

Human lysine methyltransferase Smyd3 in complex with AdoHcy (Form I)

Functional Information from GO Data
ChainGOidnamespacecontents
A0000978molecular_functionRNA polymerase II cis-regulatory region sequence-specific DNA binding
A0000993molecular_functionRNA polymerase II complex binding
A0001162molecular_functionRNA polymerase II intronic transcription regulatory region sequence-specific DNA binding
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006325biological_processchromatin organization
A0006334biological_processnucleosome assembly
A0008168molecular_functionmethyltransferase activity
A0014904biological_processmyotube cell development
A0032259biological_processmethylation
A0033138biological_processpositive regulation of peptidyl-serine phosphorylation
A0042054molecular_functionhistone methyltransferase activity
A0045184biological_processestablishment of protein localization
A0045944biological_processpositive regulation of transcription by RNA polymerase II
A0046872molecular_functionmetal ion binding
A0071549biological_processcellular response to dexamethasone stimulus
A0140939molecular_functionhistone H4 methyltransferase activity
A0140954molecular_functionhistone H3K36 dimethyltransferase activity
A0140999molecular_functionhistone H3K4 trimethyltransferase activity
B0000978molecular_functionRNA polymerase II cis-regulatory region sequence-specific DNA binding
B0000993molecular_functionRNA polymerase II complex binding
B0001162molecular_functionRNA polymerase II intronic transcription regulatory region sequence-specific DNA binding
B0005515molecular_functionprotein binding
B0005634cellular_componentnucleus
B0005654cellular_componentnucleoplasm
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006325biological_processchromatin organization
B0006334biological_processnucleosome assembly
B0008168molecular_functionmethyltransferase activity
B0014904biological_processmyotube cell development
B0032259biological_processmethylation
B0033138biological_processpositive regulation of peptidyl-serine phosphorylation
B0042054molecular_functionhistone methyltransferase activity
B0045184biological_processestablishment of protein localization
B0045944biological_processpositive regulation of transcription by RNA polymerase II
B0046872molecular_functionmetal ion binding
B0071549biological_processcellular response to dexamethasone stimulus
B0140939molecular_functionhistone H4 methyltransferase activity
B0140954molecular_functionhistone H3K36 dimethyltransferase activity
B0140999molecular_functionhistone H3K4 trimethyltransferase activity
Functional Information from PDB Data
site_idAC1
Number of Residues14
DetailsBINDING SITE FOR RESIDUE SAH A 437
ChainResidue
AARG14
AHIS206
ATYR239
ATYR257
APHE259
AHOH450
AGLY15
AASN16
ATYR124
AGLU130
AASN132
AASN181
ASER202
AASN205

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 438
ChainResidue
ACYS49
ACYS52
ACYS71
ACYS75

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 439
ChainResidue
ACYS62
ACYS65
AHIS83
ACYS87

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 440
ChainResidue
ACYS208
ACYS261
ACYS263
ACYS266

site_idAC5
Number of Residues12
DetailsBINDING SITE FOR RESIDUE SAH B 437
ChainResidue
BARG14
BGLY15
BASN16
BTYR124
BASN132
BSER202
BLEU204
BASN205
BHIS206
BTYR239
BTYR257
BPHE259

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 438
ChainResidue
BCYS49
BCYS52
BCYS71
BCYS75

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 439
ChainResidue
BCYS62
BCYS65
BHIS83
BCYS87

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 440
ChainResidue
BCYS208
BCYS261
BCYS263
BCYS266

Functional Information from PROSITE/UniProt
site_idPS01360
Number of Residues39
DetailsZF_MYND_1 Zinc finger MYND-type signature. Cdr..Cllgkeklmr........CsqCrvakYCsakCqkkawpd..Hkre.C
ChainResidueDetails
ACYS49-CYS87

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues76
DetailsZN_FING: MYND-type => ECO:0000255|PROSITE-ProRule:PRU00134
ChainResidueDetails
ACYS49-CYS87
BCYS49-CYS87

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|Ref.12
ChainResidueDetails
AARG14
AASN205
BARG14
BASN205

site_idSWS_FT_FI3
Number of Residues16
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00134
ChainResidueDetails
ACYS49
ACYS52
ACYS62
ACYS65
ACYS71
BCYS49
BCYS52
BCYS62
BCYS65
BCYS71
BCYS75
BHIS83
BCYS87
ACYS75
AHIS83
ACYS87

site_idSWS_FT_FI4
Number of Residues10
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00190, ECO:0000269|Ref.12
ChainResidueDetails
ATYR124
AASN132
AASN181
ATYR239
APHE259
BTYR124
BASN132
BASN181
BTYR239
BPHE259

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: N-acetylmethionine => ECO:0007744|PubMed:22814378
ChainResidueDetails
AMET1
BMET1

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ATHR22
BTHR22

219140

PDB entries from 2024-05-01

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