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4N3B

Crystal Structure of human O-GlcNAc Transferase bound to a peptide from HCF-1 pro-repeat2(1-26)E10Q and UDP-5SGlcNAc

Functional Information from GO Data
ChainGOidnamespacecontents
A0006493biological_processprotein O-linked glycosylation
A0016757molecular_functionglycosyltransferase activity
Functional Information from PDB Data
site_idAC1
Number of Residues31
DetailsBINDING SITE FOR RESIDUE 12V A 1501
ChainResidue
AHIS498
ATYR841
ALYS842
ALEU866
AVAL895
AALA896
ALYS898
AHIS901
AARG904
ACYS917
AHIS920
APRO559
ATHR921
ATHR922
AASP925
AHOH1611
AHOH1625
AHOH1646
AHOH1687
AHOH1696
BPRO7
BPRO8
ATHR560
BCYS9
BGLN10
ALEU563
ALEU653
AGLY654
APRO656
APHE694
AGLN839

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

site_idSWS_FT_FI2
Number of Residues33
DetailsRepeat: {"description":"TPR 10"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues33
DetailsRepeat: {"description":"TPR 11"}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues33
DetailsRepeat: {"description":"TPR 12"}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues10
DetailsRepeat: {"description":"TPR 13; truncated"}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues19
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 Residues2
DetailsMotif: {"description":"DFP motif","evidences":[{"source":"PubMed","id":"27713473","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues16
DetailsMotif: {"description":"Nuclear localization signal","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues1
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 Residues10
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"23103939","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4GYW","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues1
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 Residues1
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P56558","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI13
Number of Residues1
DetailsGlycosylation: {"description":"O-linked (GlcNAc) serine; by autocatalysis","evidences":[{"source":"PubMed","id":"27713473","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI14
Number of Residues1
DetailsSite: {"description":"Cleavage; by autolysis","evidences":[{"source":"PubMed","id":"7590226","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

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PDB entries from 2025-12-17

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