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4N3C

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

Functional Information from GO Data
ChainGOidnamespacecontents
A0006493biological_processprotein O-linked glycosylation
A0016757molecular_functionglycosyltransferase activity
Functional Information from PDB Data
site_idAC1
Number of Residues29
DetailsBINDING SITE FOR RESIDUE UD1 A 1201
ChainResidue
AHIS498
ATYR841
ALYS842
ALEU866
AVAL895
AALA896
ALYS898
AHIS901
AARG904
ACYS917
AHIS920
AHIS558
ATHR921
ATHR922
AASP925
AHOH1324
AHOH1375
BPRO7
BPRO8
BCYS9
BGLU10
BHOH101
APRO559
ATHR560
ALEU653
AGLY654
APRO656
APHE694
AGLN839

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsSITE: Cleavage; by autolysis => ECO:0000269|PubMed:7590226
ChainResidueDetails
BGLU10

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:23103939, ECO:0007744|PDB:4GYW
ChainResidueDetails
AGLN839
ALYS842
AALA896
AHIS901
AHIS920
AASP925

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphothreonine; by AMPK => ECO:0000269|PubMed:24563466, ECO:0000269|PubMed:37541260
ChainResidueDetails
ATHR444

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P56558
ChainResidueDetails
ATYR979

site_idSWS_FT_FI5
Number of Residues1
DetailsCARBOHYD: O-linked (GlcNAc) serine; by autocatalysis => ECO:0000269|PubMed:27713473
ChainResidueDetails
ASER389

223166

PDB entries from 2024-07-31

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