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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 Residues2
DetailsMOD_RES: Phosphothreonine; by CDK1 => ECO:0000269|PubMed:7592773
ChainResidueDetails
BTHR18
DTHR18

site_idSWS_FT_FI2
Number of Residues12
DetailsBINDING: BINDING => ECO:0000269|PubMed:23103939, ECO:0007744|PDB:4GYW
ChainResidueDetails
AGLN839
CHIS901
CHIS920
CASP925
ALYS842
AALA896
AHIS901
AHIS920
AASP925
CGLN839
CLYS842
CALA896

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Phosphothreonine; by AMPK => ECO:0000269|PubMed:24563466, ECO:0000269|PubMed:37541260
ChainResidueDetails
ATHR444
CTHR444

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P56558
ChainResidueDetails
ATYR979
CTYR979

site_idSWS_FT_FI5
Number of Residues2
DetailsCARBOHYD: O-linked (GlcNAc) serine; by autocatalysis => ECO:0000269|PubMed:27713473
ChainResidueDetails
ASER389
CSER389

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PDB entries from 2024-10-09

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