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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 Residues1
DetailsSITE: Cleavage; by autolysis => ECO:0000269|PubMed:7590226
ChainResidueDetails
BGLN10

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

227344

PDB entries from 2024-11-13

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