5elf

Cholera toxin El Tor B-pentamer in complex with A-pentasaccharide

Method: X-RAY DIFFRACTION Dmax: 91.1 Å Quality: EXCELLENT

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

Cholera enterotoxin subunit B

Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)

UniProt P01556

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Other combination Homooligomer Protein × 5 其他Polymer 3 PDB declaration: pentameric(5) Consistent with protein copy count Chain A; UniProt 22–124 Chain B; UniProt 22–124 Chain C; UniProt 22–124 Chain D; UniProt 22–124 Chain E; UniProt 22–124 Not recorded ;alpha-L-fucopyranose-(1-2)-[2-acetamido-2-deoxy-alpha-D-galactopyranose-(1-3)]beta-D-galactopyranose-(1-4)-[alpha-L-fucopyranose-(1-3)]alpha-D-glucopyranose ; × 2 ;alpha-L-fucopyranose-(1-2)-[2-acetamido-2-deoxy-alpha-D-galactopyranose-(1-3)]beta-D-galactopyranose-(1-4)-[alpha-L-fucopyranose-(1-3)]beta-D-glucopyranose ; × 1 CA CALCIUM ION × 10 BCN BICINE × 10 FUC alpha-L-fucopyranose × 1 GLC alpha-D-glucopyranose × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.5;293 K;0.1 M Bicine-Tris, 9% PEG1000, 9% PEG3350, 9% MPD, 0.03 M calcium chloride, 0.03 M magnesium chloride. Microseeding. Resolution 1.55 Å R-free 0.220
2 Other combination Homooligomer Protein × 5 其他Polymer 4 PDB declaration: pentameric(5) Consistent with protein copy count Chain F; UniProt 22–124 Chain G; UniProt 22–124 Chain H; UniProt 22–124 Chain I; UniProt 22–124 Chain J; UniProt 22–124 Not recorded ;alpha-L-fucopyranose-(1-2)-[2-acetamido-2-deoxy-alpha-D-galactopyranose-(1-3)]beta-D-galactopyranose-(1-4)-[alpha-L-fucopyranose-(1-3)]alpha-D-glucopyranose ; × 2 ;alpha-L-fucopyranose-(1-2)-[2-acetamido-2-deoxy-alpha-D-galactopyranose-(1-3)]beta-D-galactopyranose-(1-4)-[alpha-L-fucopyranose-(1-3)]beta-D-glucopyranose ; × 2 FUC alpha-L-fucopyranose × 1 GLC alpha-D-glucopyranose × 1 PG4 TETRAETHYLENE GLYCOL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.5;293 K;0.1 M Bicine-Tris, 9% PEG1000, 9% PEG3350, 9% MPD, 0.03 M calcium chloride, 0.03 M magnesium chloride. Microseeding. Resolution 1.55 Å R-free 0.220

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.

26 other PDB entries and 34 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CHTB_VIBCH
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–103; UniProt 22–124 Author chain B; PDBConstruct 1–103; UniProt 22–124 Author chain C; PDBConstruct 1–103; UniProt 22–124 Author chain D; PDBConstruct 1–103; UniProt 22–124 Author chain E; PDBConstruct 1–103; UniProt 22–124 Author chain F; PDBConstruct 1–103; UniProt 22–124 Author chain G; PDBConstruct 1–103; UniProt 22–124 Author chain H; PDBConstruct 1–103; UniProt 22–124 Author chain I; PDBConstruct 1–103; UniProt 22–124 Author chain J; PDBConstruct 1–103; UniProt 22–124

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 5elf

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id5elf
Deposition date deposition_date2015-11-04
Structure title titleCholera toxin El Tor B-pentamer in complex with A-pentasaccharide
Keywords keywordsCholera toxin B-pentamer, Human milk oligosaccharide, complex, blood group oligosaccharide/antigen, toxin; TOXIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier31.10
Radius of gyration Rg (electron density) rg_electron29.58
Forward intensity I(0) i0244449000.00
Molecular weight molecular_weight124910.0 kDa
Excluded volume excluded_volume156730 ų
Envelope volume envelope_volume184810 ų
Hydration-shell volume shell_volume49262 ų
Envelope diameter envelope_diameter92.7
Shell Rg shell_rg38.98
Envelope Rg envelope_rg29.41
Shape Rg shape_rg29.62
Total Rg total_rg30.29
Total atoms total_atoms8724
Residues n_residues1030
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 dmax91.1
Rg (real space) rg_real30.84
Rg uncertainty (real space) rg_real_error0.40
I(0) (real space) i0_real2.4440e+08
I(0) uncertainty (real space) i0_real_error3.0690e+06
Rg (reciprocal space) rg_reciprocal30.96
I(0) (reciprocal space) i0_reciprocal244500000.0000
Solution quality estimate total_estimate0.9073
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary42.9
Skewness Skewness skewness0.029
Kurtosis Kurtosis kurtosis-0.565
Angular range angular_range— – 0.2550 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha130000000.0000
Real-space data points n_real_points52
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.953; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.972; Smooth: 0.961

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (9)

7. Fold Classification (SCOP + CATH) 20 domains

SCOP 2.08 (10 domains)

Domain ID domain_idd5elfa_
Class classb — All beta proteins
Fold Fold foldb.40 — OB-fold
Superfamily Superfamily superfamilyb.40.2 — Bacterial enterotoxins
Family Family familyb.40.2.1 — Bacterial AB5 toxins, B-subunits
Domain ID domain_idd5elfb_
Class classb — All beta proteins
Fold Fold foldb.40 — OB-fold
Superfamily Superfamily superfamilyb.40.2 — Bacterial enterotoxins
Family Family familyb.40.2.1 — Bacterial AB5 toxins, B-subunits
Domain ID domain_idd5elfc_
Class classb — All beta proteins
Fold Fold foldb.40 — OB-fold
Superfamily Superfamily superfamilyb.40.2 — Bacterial enterotoxins
Family Family familyb.40.2.1 — Bacterial AB5 toxins, B-subunits
Domain ID domain_idd5elfd_
Class classb — All beta proteins
Fold Fold foldb.40 — OB-fold
Superfamily Superfamily superfamilyb.40.2 — Bacterial enterotoxins
Family Family familyb.40.2.1 — Bacterial AB5 toxins, B-subunits
Domain ID domain_idd5elfe_
Class classb — All beta proteins
Fold Fold foldb.40 — OB-fold
Superfamily Superfamily superfamilyb.40.2 — Bacterial enterotoxins
Family Family familyb.40.2.1 — Bacterial AB5 toxins, B-subunits
Domain ID domain_idd5elff_
Class classb — All beta proteins
Fold Fold foldb.40 — OB-fold
Superfamily Superfamily superfamilyb.40.2 — Bacterial enterotoxins
Family Family familyb.40.2.1 — Bacterial AB5 toxins, B-subunits
Domain ID domain_idd5elfg_
Class classb — All beta proteins
Fold Fold foldb.40 — OB-fold
Superfamily Superfamily superfamilyb.40.2 — Bacterial enterotoxins
Family Family familyb.40.2.1 — Bacterial AB5 toxins, B-subunits
Domain ID domain_idd5elfh_
Class classb — All beta proteins
Fold Fold foldb.40 — OB-fold
Superfamily Superfamily superfamilyb.40.2 — Bacterial enterotoxins
Family Family familyb.40.2.1 — Bacterial AB5 toxins, B-subunits
Domain ID domain_idd5elfi_
Class classb — All beta proteins
Fold Fold foldb.40 — OB-fold
Superfamily Superfamily superfamilyb.40.2 — Bacterial enterotoxins
Family Family familyb.40.2.1 — Bacterial AB5 toxins, B-subunits
Domain ID domain_idd5elfj_
Class classb — All beta proteins
Fold Fold foldb.40 — OB-fold
Superfamily Superfamily superfamilyb.40.2 — Bacterial enterotoxins
Family Family familyb.40.2.1 — Bacterial AB5 toxins, B-subunits

CATH v4.4 (10 domains)

Domain ID domain_id5elfA00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily110
Domain ID domain_id5elfB00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily110
Domain ID domain_id5elfC00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily110
Domain ID domain_id5elfD00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily110
Domain ID domain_id5elfE00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily110
Domain ID domain_id5elfF00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily110
Domain ID domain_id5elfG00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily110
Domain ID domain_id5elfH00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily110
Domain ID domain_id5elfI00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily110
Domain ID domain_id5elfJ00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily110

8. Citations (1)

9. Files and Curves (10)