6EOU: PDB entry 6EOU

Name: PDB 6EOU: O-GlcNAc transferase TPR domain with the intellectual disability associated mutation L254F
Published: 2018-05-09
License: https://creativecommons.org/publicdomain/zero/1.0/
Keywords: transferase

O-GlcNAc transferase TPR domain with the intellectual disability associated mutation L254F. Determined by X-ray diffraction at 1.75 Å resolution. Released 9 May 2018.

Method: X-ray diffraction
Resolution: 1.75 Å
Organism: Homo sapiens
Chains: 1
Atoms: 2,988
Mol. weight: 43.54 kDa
Released: 9 May 2018

Explore 6EOU in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6EOU contains 21 α-helices and 0 β-strands across 1 chain. 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: 21 helices, 0 β-strands

Element	Residues	Length
α-helix	60-67	8
α-helix	71-83	13
α-helix	89-101	13
α-helix	105-118	14
α-helix	123-135	13
α-helix	139-152	14
α-helix	157-169	13
α-helix	173-186	14
α-helix	191-203	13
α-helix	207-220	14
α-helix	225-237	13
α-helix	241-254	14
α-helix	259-271	13
α-helix	275-288	14
α-helix	293-306	14
α-helix	309-322	14
α-helix	327-340	14
α-helix	343-356	14
α-helix	361-373	13
α-helix	377-390	14
α-helix	393-399	7

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit	A	protein	388	Homo sapiens	O15294 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>6EOU_1 UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit (chains A)
GPMELAHREYQAGDFEAAERHCMQLWRQEPDNTGVLLLLSSIHFQCRRLDRSAHFSTLAI
KQNPLLAEAYSNLGNVYKERGQLQEAIEHYRHALRLKPDFIDGYINLAAALVAAGDMEGA
VQAYVSALQYNPDLYCVRSDLGNLLKALGRLEEAKACYLKAIETQPNFAVAWSNLGCVFN
AQGEIWLAIHHFEKAVTLDPNFLDAYINLGNVLKEARIFDRAVAAYLRALSFSPNHAVVH
GNLACVYYEQGLIDLAIDTYRRAIELQPHFPDAYCNLANALKEKGSVAEAEDCYNTALRL
CPTHADSLNNLANIKREQGNIEEAVRLYRKALEVFPEFAAAHSNLASVLQQQGKLQEALM
HYKEAIRISPTFADAYSNMGNTLKEMQD

Primary citation

The O-GlcNAc Transferase Intellectual Disability Mutation L254F Distorts the TPR Helix. Gundogdu, M., Llabres, S., Gorelik, A. et al. Cell Chem Biol (2018) 25:513-518.e4. DOI 10.1016/j.chembiol.2018.03.004 · PubMed

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
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
6MA3 2.0 Å, Crystal structure of human O-GlcNAc transferase bound to a peptide from HCF-1 pro-repeat…

Browse structure collections

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