1lt6

HEAT-LABILE ENTEROTOXIN B-PENTAMER COMPLEXED WITH METANITROPHENYLGALACTOSIDE

Method: X-RAY DIFFRACTION

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

HEAT-LABILE ENTEROTOXIN

Escherichia coli

UniProt P32890

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein homooligomer Homooligomer Protein 5 3-nitrophenyl alpha-D-galactopyranoside × 5 water × 5 Consistent with protein count
2 Protein homooligomer Homooligomer Protein 5 3-nitrophenyl alpha-D-galactopyranoside × 5 water × 5 Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name ELBP_ECOLI
Isoform
PDB entities 1
Chains and sequence ranges 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 L; PDBConstruct 1–103; UniProt 22–124 Author chain M; PDBConstruct 1–103; UniProt 22–124 Author chain N; PDBConstruct 1–103; UniProt 22–124 Author chain O; PDBConstruct 1–103; UniProt 22–124 Author chain P; 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.

2. Structure Basics 2. Structure Basics

Entry ID entry_id1lt6
Deposition date deposition_date1997-10-01
Structure title titleHEAT-LABILE ENTEROTOXIN B-PENTAMER COMPLEXED WITH METANITROPHENYLGALACTOSIDE
Keywords keywordsENTEROTOXIN; ENTEROTOXIN
Experimental Method methodX-RAY DIFFRACTION

3. Official assembly/model SAXS Official SAXS Profiles

This page reads only the latest assembly calculations. Every curve maps to an explicit PDB entry, official biological assembly and coordinate model.

1lt6__assembly_2__model_1

Assembly 2 · Model 1 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

1lt6__assembly_2__model_1 | I(q)

10-2 10-1 105 106 107 q (1/Angstrom) I(q)
100 plotted points; both axes use logarithmic scales.

1lt6__assembly_2__model_1 | P(r) · Pending

The new assembly/model P(r) has not been calculated yet This placeholder does not display legacy data r (Angstrom) P(r)
P(r) will be calculated and displayed separately for the same assembly/model.
Rg(Guinier)24.80 Å
Rg (electron density)23.53 Å
Total Rg24.30 Å
Atom count4225
Residues515
Excluded volume75674 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 1lt6__assembly_1__model_1 pentameric (5) Success 4.1.3-1-20251215 (887e7ef) View Download
2 1 1lt6__assembly_2__model_1 pentameric (5) Success 4.1.3-1-20251215 (887e7ef) View Download

4. Crystallography and Experiment 4. Crystallography & Experiment

5. Entities and Polymers Entities & Polymers (3)

6. Fold Classification (SCOP + CATH) 20 domains

SCOP 2.08 (10 domains)

Domain ID domain_idd1lt6d_
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_idd1lt6e_
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_idd1lt6f_
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_idd1lt6g_
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_idd1lt6h_
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_idd1lt6l_
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_idd1lt6m_
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_idd1lt6n_
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_idd1lt6o_
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_idd1lt6p_
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_id1lt6D00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily110
Domain ID domain_id1lt6E00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily110
Domain ID domain_id1lt6F00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily110
Domain ID domain_id1lt6G00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily110
Domain ID domain_id1lt6H00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily110
Domain ID domain_id1lt6L00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily110
Domain ID domain_id1lt6M00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily110
Domain ID domain_id1lt6N00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily110
Domain ID domain_id1lt6O00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily110
Domain ID domain_id1lt6P00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily110

7. Citations (3)