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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 Residues4
DetailsACT_SITE: Proton acceptor => ECO:0000305|PubMed:21240259, ECO:0000305|PubMed:26678539
ChainResidueDetails
AHIS498
BHIS498
CHIS498
DHIS498

site_idSWS_FT_FI2
Number of Residues24
DetailsBINDING: BINDING => ECO:0000269|PubMed:23103939, ECO:0007744|PDB:4GYW
ChainResidueDetails
AGLN839
BHIS901
BHIS920
BASP925
CGLN839
CLYS842
CALA896
CHIS901
CHIS920
CASP925
DGLN839
ALYS842
DLYS842
DALA896
DHIS901
DHIS920
DASP925
AALA896
AHIS901
AHIS920
AASP925
BGLN839
BLYS842
BALA896

site_idSWS_FT_FI3
Number of Residues4
DetailsMOD_RES: Phosphothreonine; by AMPK => ECO:0000269|PubMed:24563466, ECO:0000269|PubMed:37541260
ChainResidueDetails
ATHR444
BTHR444
CTHR444
DTHR444

site_idSWS_FT_FI4
Number of Residues4
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P56558
ChainResidueDetails
ATYR979
BTYR979
CTYR979
DTYR979

site_idSWS_FT_FI5
Number of Residues4
DetailsCARBOHYD: O-linked (GlcNAc) serine; by autocatalysis => ECO:0000269|PubMed:27713473
ChainResidueDetails
ASER389
BSER389
CSER389
DSER389

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PDB entries from 2024-10-09

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