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3PE3

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
B0006493biological_processprotein O-linked glycosylation
B0016757molecular_functionglycosyltransferase activity
C0006493biological_processprotein O-linked glycosylation
C0016757molecular_functionglycosyltransferase activity
D0006493biological_processprotein O-linked glycosylation
D0016757molecular_functionglycosyltransferase activity
Functional Information from PDB Data
site_idAC1
Number of Residues17
DetailsBINDING SITE FOR RESIDUE UDP A 1201
ChainResidue
AHOH14
ALYS898
AHIS901
AARG904
AGLY919
AHIS920
ATHR921
ATHR922
AASP925
AHOH136
AHOH248
AHOH261
AGLN839
ALYS842
ALEU866
AVAL895
AALA896

site_idAC2
Number of Residues15
DetailsBINDING SITE FOR RESIDUE UDP B 1201
ChainResidue
BHOH1
BHOH16
BPRO559
BGLN839
BLYS842
BLEU866
BVAL895
BALA896
BLYS898
BHIS901
BARG904
BHIS920
BTHR921
BTHR922
BASP925

site_idAC3
Number of Residues14
DetailsBINDING SITE FOR RESIDUE UDP C 1201
ChainResidue
CHOH262
CPRO559
CGLN839
CLYS842
CLEU866
CVAL895
CALA896
CLYS898
CHIS901
CARG904
CHIS920
CTHR921
CTHR922
CASP925

site_idAC4
Number of Residues15
DetailsBINDING SITE FOR RESIDUE UDP D 1201
ChainResidue
DHOH4
DHOH73
DASN838
DGLN839
DLYS842
DLEU866
DVAL895
DALA896
DLYS898
DHIS901
DARG904
DHIS920
DTHR921
DTHR922
DASP925

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues132
DetailsRepeat: {"description":"TPR 9"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues132
DetailsRepeat: {"description":"TPR 10"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues132
DetailsRepeat: {"description":"TPR 11"}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues132
DetailsRepeat: {"description":"TPR 12"}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues40
DetailsRepeat: {"description":"TPR 13; truncated"}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues76
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 Residues8
DetailsMotif: {"description":"DFP motif","evidences":[{"source":"PubMed","id":"27713473","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues64
DetailsMotif: {"description":"Nuclear localization signal","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues4
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 Residues40
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"23103939","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4GYW","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues4
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 Residues4
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P56558","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI13
Number of Residues4
DetailsGlycosylation: {"description":"O-linked (GlcNAc) serine; by autocatalysis","evidences":[{"source":"PubMed","id":"27713473","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

246333

PDB entries from 2025-12-17

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