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3PE4

Structure of human O-GlcNAc transferase and its complex with a peptide substrate

Functional Information from GO Data
ChainGOidnamespacecontents
A0006493biological_processprotein O-linked glycosylation
A0016757molecular_functionglycosyltransferase activity
C0006493biological_processprotein O-linked glycosylation
C0016757molecular_functionglycosyltransferase activity
Functional Information from PDB Data
site_idAC1
Number of Residues21
DetailsBINDING SITE FOR RESIDUE UDP A 1212
ChainResidue
AHOH4
AARG904
AHIS920
ATHR921
ATHR922
AASP925
AHOH1064
AHOH1087
BTHR18
BVAL20
BSER21
APRO559
BHOH27
BHOH57
AGLN839
ALYS842
ALEU866
AVAL895
AALA896
ALYS898
AHIS901

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 5
ChainResidue
AGLY365
ALYS366
ALEU367
AGLN368
AHOH1070

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 B 1
ChainResidue
AGLY635
AHOH1103
BASN24
BMET25

site_idAC4
Number of Residues22
DetailsBINDING SITE FOR RESIDUE UDP C 1212
ChainResidue
CHOH9
CPRO559
CGLN839
CLYS842
CLEU866
CVAL895
CALA896
CLYS898
CHIS901
CARG904
CHIS920
CTHR921
CTHR922
CASP925
CHOH1060
CHOH1086
CHOH1254
DTHR18
DVAL20
DSER21
DHOH32
DHOH98

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 D 3
ChainResidue
CGLY635
CHOH1182
DASN24
DMET25

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues33
DetailsRepeat: {"description":"TPR 9"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues66
DetailsRepeat: {"description":"TPR 10"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues66
DetailsRepeat: {"description":"TPR 11"}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues66
DetailsRepeat: {"description":"TPR 12"}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues20
DetailsRepeat: {"description":"TPR 13; truncated"}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues38
DetailsRegion: {"description":"Required for phosphatidylinositol 3,4,5-triphosphate binding","evidences":[{"source":"UniProtKB","id":"P56558","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues4
DetailsMotif: {"description":"DFP motif","evidences":[{"source":"PubMed","id":"27713473","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues32
DetailsMotif: {"description":"Nuclear localization signal","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues2
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"21240259","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"26678539","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues20
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"23103939","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4GYW","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues2
DetailsModified residue: {"description":"Phosphothreonine; by AMPK","evidences":[{"source":"PubMed","id":"24563466","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"37541260","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues2
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P56558","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI13
Number of Residues2
DetailsGlycosylation: {"description":"O-linked (GlcNAc) serine; by autocatalysis","evidences":[{"source":"PubMed","id":"27713473","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI14
Number of Residues2
DetailsModified residue: {"description":"Phosphothreonine; by CDK1","evidences":[{"source":"PubMed","id":"7592773","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

245663

PDB entries from 2025-12-03

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