6eou

O-GlcNAc transferase TPR domain with the intellectual disability associated mutation L254F

Method: X-RAY DIFFRACTION Dmax: 95.5 Å Quality: GOOD

1. Protein Identity and Related Structures Protein Identity & Related Structures

UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit

Homo sapiens

UniProt O15294

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 26–410 Mutation:L254F No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.5;295.2 K;0.1 M Na-HEPES and 0.1 M MOPS-HCl pH 7,5, 0.04 M diethylene glycol, 0.04 M triethylene glycol, 0.04 M tetraethylene glycol, 0.04 M pentaethylene glycol, 20 % v/v ethylene glycol and 10 % w/v PEG 4000 Resolution 1.75 Å R-free 0.227

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

43 other PDB entries and 101 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name OGT1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 4–388; UniProt 26–410

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

SAXS scattering curve SAXS Profile

SAXS profile for 6eou

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6eou
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6eou
Deposition date deposition_date2017-10-10
Structure title titleO-GlcNAc transferase TPR domain with the intellectual disability associated mutation L254F
Keywords keywordsintellectual disability associated point mutation in O-GlcNAc transferase tetratricopeptide domain, TRANSFERASE; TRANSFERASE
Experimental Method methodX-RAY DIFFRACTION

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier28.90
Radius of gyration Rg (electron density) rg_electron28.63
Forward intensity I(0) i023901400.00
Molecular weight molecular_weight38128.0 kDa
Excluded volume excluded_volume47738 ų
Envelope volume envelope_volume64280 ų
Hydration-shell volume shell_volume20178 ų
Envelope diameter envelope_diameter99.9
Shell Rg shell_rg33.85
Envelope Rg envelope_rg27.70
Shape Rg shape_rg28.62
Total Rg total_rg29.23
Total atoms total_atoms2692
Residues n_residues343
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 −1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax95.5
Rg (real space) rg_real29.07
Rg uncertainty (real space) rg_real_error0.94
I(0) (real space) i0_real2.3900e+07
I(0) uncertainty (real space) i0_real_error4.1710e+05
Rg (reciprocal space) rg_reciprocal29.00
I(0) (reciprocal space) i0_reciprocal23900000.0000
Solution quality estimate total_estimate0.8547
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary33.0
Skewness Skewness skewness0.344
Kurtosis Kurtosis kurtosis-0.620
Angular range angular_range— – 0.2750 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1342000.0000
Real-space data points n_real_points56
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.881; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.622; Smooth: 0.844

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id6eouA00
Class class1 — Mainly Alpha
Architecture architecture25 — Alpha Horseshoe
Topology topology40 — Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat
Homologous superfamily homologous superfamily10 — Tetratricopeptide repeat domain

8. Citations (1)

9. Files and Curves (10)