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5V37

Crystal structure of SMYD3 with SAM and EPZ028862

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
Functional Information from PDB Data
site_idAC1
Number of Residues5
Detailsbinding site for residue ZN A 501
ChainResidue
ACYS49
ACYS52
ACYS71
ACYS75
AHOH658

site_idAC2
Number of Residues4
Detailsbinding site for residue ZN A 502
ChainResidue
ACYS208
ACYS261
ACYS263
ACYS266

site_idAC3
Number of Residues4
Detailsbinding site for residue ZN A 503
ChainResidue
ACYS62
ACYS65
AHIS83
ACYS87

site_idAC4
Number of Residues23
Detailsbinding site for residue SAM A 504
ChainResidue
AARG14
AGLY15
AASN16
ATYR124
AGLU130
AASN132
ACYS180
AASN181
ASER202
ALEU203
ALEU204
AASN205
AHIS206
ATYR239
ATYR257
APHE259
AHOH666
AHOH669
AHOH679
AHOH753
AHOH810
AHOH814
AHOH879

site_idAC5
Number of Residues19
Detailsbinding site for residue 8WD A 505
ChainResidue
ACYS180
AASN181
ASER182
APHE183
ATHR184
AMET190
AGLU192
AILE237
ATYR239
AASP241
ATYR257
AVAL368
ADMS507
AHOH627
AHOH651
AHOH681
AHOH795
AHOH928
AHOH942

site_idAC6
Number of Residues8
Detailsbinding site for residue PEG A 506
ChainResidue
AALA10
ATHR11
AASN13
AARG14
AGLY15
AGLU318
AHOH663
AHOH821

site_idAC7
Number of Residues4
Detailsbinding site for residue DMS A 507
ChainResidue
ASER182
ATHR184
AGLN256
A8WD505

site_idAC8
Number of Residues5
Detailsbinding site for residue DMS A 508
ChainResidue
APRO99
AMET113
AASP114
AGLY115
ATHR150

site_idAC9
Number of Residues7
Detailsbinding site for residue EDO A 509
ChainResidue
AALA188
AGLU189
AVAL371
ALYS375
ALEU410
AHOH624
AHOH944

site_idAD1
Number of Residues4
Detailsbinding site for residue EDO A 510
ChainResidue
AASP139
ALYS140
AHOH665
AHOH891

site_idAD2
Number of Residues4
Detailsbinding site for residue EDO A 511
ChainResidue
AARG359
AARG369
AHOH737
AHOH842

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 Residues38
DetailsZN_FING: MYND-type => ECO:0000255|PROSITE-ProRule:PRU00134
ChainResidueDetails
ACYS49-CYS87

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|Ref.12
ChainResidueDetails
AARG14
AASN205

site_idSWS_FT_FI3
Number of Residues8
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00134
ChainResidueDetails
ACYS49
ACYS52
ACYS62
ACYS65
ACYS71
ACYS75
AHIS83
ACYS87

site_idSWS_FT_FI4
Number of Residues5
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00190, ECO:0000269|Ref.12
ChainResidueDetails
ATYR124
AASN132
AASN181
ATYR239
APHE259

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: N-acetylmethionine => ECO:0007744|PubMed:22814378
ChainResidueDetails
AMET1

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ATHR22

222624

PDB entries from 2024-07-17

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