5ub5

human POGLUT1 in complex with human Notch1 EGF12 S458T mutant and UDP

Method: X-RAY DIFFRACTION Dmax: 72.9 Å Quality: REASONABLE

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

Protein O-glucosyltransferase 1

Homo sapiens

UniProt Q8NBL1

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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 29–385 Fragment:UNP residues 29-385 Neurogenic locus notch homolog protein 1 × 1 (P46531) NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 3 UDP URIDINE-5'-DIPHOSPHATE × 1 CA CALCIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;295 K;20% (v/v) PEG5000 MME, 50 mM MES pH 6.5, 2mM CaCl2, 250mM NaCl, 5% (v/v) 2-methyl-2,4-pentanediol Resolution 2.09 Å R-free 0.193

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.

5 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PGLT1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–357; UniProt 29–385

Neurogenic locus notch homolog protein 1

Homo sapiens

UniProt P46531

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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 452–491 Fragment:UNP residues 452-491 Protein O-glucosyltransferase 1 × 1 (Q8NBL1) NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 3 UDP URIDINE-5'-DIPHOSPHATE × 1 CA CALCIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;295 K;20% (v/v) PEG5000 MME, 50 mM MES pH 6.5, 2mM CaCl2, 250mM NaCl, 5% (v/v) 2-methyl-2,4-pentanediol Resolution 2.09 Å R-free 0.193

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.

27 other PDB entries and 35 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NOTC1_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 3–42; UniProt 452–491

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 5ub5

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5ub5
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5ub5
Deposition date deposition_date2016-12-20
Structure title titlehuman POGLUT1 in complex with human Notch1 EGF12 S458T mutant and UDP
Keywords keywordstransferase, glycosyltransferase, GT-B glucosyltransferase; TRANSFERASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier22.61
Radius of gyration Rg (electron density) rg_electron21.64
Forward intensity I(0) i037906400.00
Molecular weight molecular_weight47131.0 kDa
Excluded volume excluded_volume58710 ų
Envelope volume envelope_volume68118 ų
Hydration-shell volume shell_volume25722 ų
Envelope diameter envelope_diameter74.8
Shell Rg shell_rg29.04
Envelope Rg envelope_rg22.05
Shape Rg shape_rg21.59
Total Rg total_rg22.67
Total atoms total_atoms6466
Residues n_residues396
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 dmax72.9
Rg (real space) rg_real22.52
Rg uncertainty (real space) rg_real_error0.34
I(0) (real space) i0_real3.7910e+07
I(0) uncertainty (real space) i0_real_error4.7300e+05
Rg (reciprocal space) rg_reciprocal22.54
I(0) (reciprocal space) i0_reciprocal37910000.0000
Solution quality estimate total_estimate0.7173
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary27.6
Skewness Skewness skewness0.246
Kurtosis Kurtosis kurtosis-0.345
Angular range angular_range— – 0.3500 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha6984000.0000
Real-space data points n_real_points67
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.872; Stabil: 1.000; Sysdev: 0.242; Positv: 1.000; Valcen: 0.996; Smooth: 0.981

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd5ub5b_
Class classg — Small proteins
Fold Fold foldg.3 — Knottins (small inhibitors, toxins, lectins)
Superfamily Superfamily superfamilyg.3.11 — EGF/Laminin
Family Family familyg.3.11.0 — automated matches

CATH v4.4 (1 domains)

Domain ID domain_id5ub5B00
Class class2 — Mainly Beta
Architecture architecture10 — Ribbon
Topology topology25 — Laminin
Homologous superfamily homologous superfamily10 — Laminin

8. Citations (1)

9. Files and Curves (10)