1w3b

The superhelical TPR domain of O-linked GlcNAc transferase reveals structural similarities to importin alpha.

Method: X-RAY DIFFRACTION Dmax: 113.3 Å Quality: GOOD

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

UDP-N-ACETYLGLUCOSAMINE--PEPTIDE N-ACETYLGLUCOSAMINYLTRANSFERASE 110

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 homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 16–400 Chain B; UniProt 16–400 Fragment:TPR DOMAIN, RESIDUES 16-400 CA CALCIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:pH 7.5;0.1M HEPES-NA/HCL PH 7.5 0.2M CACL2 36% PEG 400 Resolution 2.85 Å R-free 0.297

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 16–400 Author chain B; PDBConstruct 4–388; UniProt 16–400

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 1w3b

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1w3b
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1w3b
Deposition date deposition_date2004-07-14
Structure title titleThe superhelical TPR domain of O-linked GlcNAc transferase reveals structural similarities to importin alpha.
Keywords keywordsOGT, GLCNAC, NUCLEOPORIN, O-LINKED GLYCOSYLATION, TPR REPEAT, PROTEIN BINDING, SIGNAL TRANSDUCTION, TRANSFERASE; TRANSFERASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier38.30
Radius of gyration Rg (electron density) rg_electron37.60
Forward intensity I(0) i0103282000.00
Molecular weight molecular_weight78916.0 kDa
Excluded volume excluded_volume97661 ų
Envelope volume envelope_volume145220 ų
Hydration-shell volume shell_volume34919 ų
Envelope diameter envelope_diameter117.9
Shell Rg shell_rg39.82
Envelope Rg envelope_rg36.90
Shape Rg shape_rg37.59
Total Rg total_rg37.82
Total atoms total_atoms5569
Residues n_residues756
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 dmax113.3
Rg (real space) rg_real38.20
Rg uncertainty (real space) rg_real_error0.86
I(0) (real space) i0_real1.0330e+08
I(0) uncertainty (real space) i0_real_error1.6050e+06
Rg (reciprocal space) rg_reciprocal38.27
I(0) (reciprocal space) i0_reciprocal103300000.0000
Solution quality estimate total_estimate0.8737
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary44.2
Skewness Skewness skewness0.074
Kurtosis Kurtosis kurtosis-0.741
Angular range angular_range— – 0.2050 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha2924000.0000
Real-space data points n_real_points42
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.998; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.992; Smooth: 0.369

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1w3ba_
Class classa — All alpha proteins
Fold Fold folda.118 — alpha-alpha superhelix
Superfamily Superfamily superfamilya.118.8 — TPR-like
Family Family familya.118.8.1 — Tetratricopeptide repeat (TPR)
Domain ID domain_idd1w3bb_
Class classa — All alpha proteins
Fold Fold folda.118 — alpha-alpha superhelix
Superfamily Superfamily superfamilya.118.8 — TPR-like
Family Family familya.118.8.1 — Tetratricopeptide repeat (TPR)

CATH v4.4 (2 domains)

Domain ID domain_id1w3bA00
Class class1 — Mainly Alpha
Architecture architecture25 — Alpha Horseshoe
Topology topology40 — Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat
Homologous superfamily homologous superfamily10 — Tetratricopeptide repeat domain
Domain ID domain_id1w3bB00
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)