5l0r

human POGLUT1 in complex with Notch1 EGF12 and UDP

Method: X-RAY DIFFRACTION Dmax: 72.3 Å Quality: GOOD

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 Not recorded Neurogenic locus notch homolog protein 1 × 1 (P46531) NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 UDP URIDINE-5'-DIPHOSPHATE × 1 GOL GLYCEROL × 1 CL CHLORIDE ION × 1 CA CALCIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;295 K;20% PEG5000 MME, 50 mM MES pH 6.5, 2mM CaCl2, 250mM NaCl, 5% glycerol Resolution 1.50 Å R-free 0.171

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 Not recorded Protein O-glucosyltransferase 1 × 1 (Q8NBL1) NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 UDP URIDINE-5'-DIPHOSPHATE × 1 GOL GLYCEROL × 1 CL CHLORIDE ION × 1 CA CALCIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;295 K;20% PEG5000 MME, 50 mM MES pH 6.5, 2mM CaCl2, 250mM NaCl, 5% glycerol Resolution 1.50 Å R-free 0.171

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 5l0r

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5l0r
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5l0r
Deposition date deposition_date2016-07-28
Structure title titlehuman POGLUT1 in complex with Notch1 EGF12 and UDP
Keywords keywordstransferase glycosyltransferase GT-B glucosyltransferase, TRANSFERASE; TRANSFERASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier22.42
Radius of gyration Rg (electron density) rg_electron21.49
Forward intensity I(0) i037673500.00
Molecular weight molecular_weight47098.0 kDa
Excluded volume excluded_volume58710 ų
Envelope volume envelope_volume67522 ų
Hydration-shell volume shell_volume25625 ų
Envelope diameter envelope_diameter75.3
Shell Rg shell_rg28.82
Envelope Rg envelope_rg21.88
Shape Rg shape_rg21.45
Total Rg total_rg22.49
Total atoms total_atoms6459
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 dmax72.3
Rg (real space) rg_real22.33
Rg uncertainty (real space) rg_real_error0.40
I(0) (real space) i0_real3.7670e+07
I(0) uncertainty (real space) i0_real_error4.8300e+05
Rg (reciprocal space) rg_reciprocal22.35
I(0) (reciprocal space) i0_reciprocal37670000.0000
Solution quality estimate total_estimate0.8898
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary27.4
Skewness Skewness skewness0.236
Kurtosis Kurtosis kurtosis-0.361
Angular range angular_range— – 0.3550 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha7449000.0000
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: 1.000; Positv: 1.000; Valcen: 0.996; Smooth: 0.952

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (8)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd5l0rb_
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_id5l0rB00
Class class2 — Mainly Beta
Architecture architecture10 — Ribbon
Topology topology25 — Laminin
Homologous superfamily homologous superfamily10 — Laminin

8. Citations (1)

9. Files and Curves (10)