5HGV: O-GlcNAc transferase point mutant, D554N

Structure of an O-GlcNAc transferase point mutant, D554N in complex with peptide. Determined by X-ray diffraction at 2.05 Å resolution. Released 14 Sept 2016.

Method

X-ray diffraction

Resolution

2.05 Å

Organism

Homo sapiens

Chains

4

Atoms

11,958

Mol. weight

165.69 kDa

Ligands

UDP, NAG

Released

14 Sept 2016

Explore 5HGV in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5HGV contains 87 α-helices and 48 β-strands across 4 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 43 helices, 23 β-strands

Molecules and chains

>5HGV_1 UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit (chains A, C)
CPTHADSLNNLANIKREQGNIEEAVRLYRKALEVFPEFAAAHSNLASVLQQQGKLQEALM
HYKEAIRISPTFADAYSNMGNTLKEMQDVQGALQCYTRAIQINPAFADAHSNLASIHKDS
GNIPEAIASYRTALKLKPDFPDAYCNLAHCLQIVCDWTDYDERMKKLVSIVADQLEKNRL
PSVHPHHSMLYPLSHGFRKAIAERHGNLCLDKINVLHKPPYEHPKDLKLSDGRLRVGYVS
SNFGNHPTSHLMQSIPGMHNPDKFEVFCYALSPDDGTNFRVKVMAEANHFIDLSQIPCNG
KAADRIHQDGIHILVNMNGYTKGARNELFALRPAPIQAMWLGYPGTSGALFMDYIITDQE
TSPAEVAEQYSEKLAYMPHTFFIGDHANMFPHLKKKAVIDFKSNGHIYDNRIVLNGIDLK
AFLDSLPDVKIVKMKCPDGGDNADSSNTALNMPVIPMNTIAEAVIEMINRGQIQITINGF
SISNGLATTQINNKAATGEEVPRTIIVTTRSQYGLPEDAIVYCNFNQLYKIDPSTLQMWA
NILKRVPNSVLWLLRFPAVGEPNIQQYAQNMGLPQNRIIFSPVAPKEEHVRRGQLADVCL
DTPLCNGHTTGMDVLWAGTPMVTMPGETLASRVAASQLTCLGCLELIAKNRQEYEDIAVK
LGTDLEYLKKVRGKVWKQRISSPLFNTKQYTMELERLYLQMWEHYAAGNKPDHMIKPVE

>5HGV_2 TYR-PRO-GLY-GLY-SER-THR-PRO-VAL-SER-SER-ALA-ASN-MET-MET (chains B, D)
YPGGSTPVSSANMM

Ligands and cofactors

Water and common crystallization additives (SO4) are not listed.

Primary citation

How the glycosyltransferase OGT catalyzes amide bond cleavage. Janetzko, J., Trauger, S.A., Lazarus, M.B. et al. Nat Chem Biol (2016) 12:899-901. DOI 10.1038/nchembio.2173 · PubMed

Related structures

Other PDB entries of the same protein (UniProt O15294 (AlphaFold model), which also has an AlphaFold model), best resolution first:

• 5NPS 1.68 Å, The human O-GlcNAc transferase in complex with a bisubstrate inhibitor
• 4GYW 1.7 Å, Crystal structure of human O-GlcNAc Transferase in complex with UDP and a glycopeptide
• 6EOU 1.75 Å, O-GlcNAc transferase TPR domain with the intellectual disability associated mutation L254F
• 4N39 1.76 Å, Crystal structure of human O-GlcNAc transferase bound to a peptide from HCF-1 pro-repeat…
• 4GYY 1.85 Å, Crystal structure of human O-GlcNAc Transferase with UDP-5SGlcNAc and a peptide substrate
• 5NPR 1.85 Å, The human O-GlcNAc transferase in complex with a thiol-linked bisubstrate inhibitor
• 3TAX 1.88 Å, A Neutral Diphosphate Mimic Crosslinks the Active Site of Human O-GlcNAc Transferase
• 4N3A 1.88 Å, Crystal Structure of human O-GlcNAc transferase bound to a peptide from HCF-1 pro-repeat…
• 4GZ3 1.9 Å, Crystal structure of human O-GlcNAc Transferase with UDP and a thioglycopeptide
• 5LWV 1.9 Å, Human OGT in complex with UDP and fused substrate peptide (HCF1)
• 6TKA 1.91 Å, Crystal structure of human O-GlcNAc transferase bound to substrate 7 and a peptide from…
• 3PE4 1.95 Å, Structure of human O-GlcNAc transferase and its complex with a peptide substrate

Browse structure collections

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