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6MA3

Crystal structure of human O-GlcNAc transferase bound to a peptide from HCF-1 pro-repeat 2 (11-26) and inhibitor 2a

Functional Information from GO Data
ChainGOidnamespacecontents
A0006493biological_processprotein O-linked glycosylation
A0016757molecular_functionglycosyltransferase activity
Functional Information from PDB Data
site_idAC1
Number of Residues19
Detailsbinding site for residue JAJ A 1101
ChainResidue
AHIS558
AALA896
ALYS898
AHIS901
AARG904
ATHR921
AHOH1270
AHOH1333
AHOH1353
AHOH1364
AHOH1466
APRO559
AHIS562
APHE837
AGLN839
ALYS842
ALEU866
APHE868
AVAL895

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000305|PubMed:21240259, ECO:0000305|PubMed:26678539
ChainResidueDetails
AHIS624

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:23103939, ECO:0007744|PDB:4GYW
ChainResidueDetails
AASP968
ALYS1022
AILE1027
AGLU965

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphothreonine; by AMPK => ECO:0000269|PubMed:24563466, ECO:0000269|PubMed:37541260
ChainResidueDetails
AMET570

site_idSWS_FT_FI4
Number of Residues1
DetailsCARBOHYD: O-linked (GlcNAc) serine; by autocatalysis => ECO:0000269|PubMed:27713473
ChainResidueDetails
AGLU515

221051

PDB entries from 2024-06-12

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