SAXSdb — 1ltr

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

HEAT-LABILE ENTEROTOXIN

Escherichia coli

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 × 5 PDB declaration: pentameric（5） Consistent with protein copy count	Chain D； UniProt 22–123 Chain E； UniProt 22–123 Chain F； UniProt 22–123 Chain G； UniProt 22–123 Chain H； UniProt 22–123	Fragment：SUBUNIT B-R2 Mutation：N103K	SO4 SULFATE ION × 6	X-RAY DIFFRACTION X-ray crystallization conditions：pH 6；pH 6	Resolution 3.04 Å R-free 0.217
2	Protein homooligomer Homooligomer Protein × 10 PDB declaration: decameric（10） Consistent with protein copy count	Chain D； UniProt 22–123 Chain E； UniProt 22–123 Chain F； UniProt 22–123 Chain G； UniProt 22–123 Chain H； UniProt 22–123	Fragment：SUBUNIT B-R2 Mutation：N103K	SO4 SULFATE ION × 12	X-RAY DIFFRACTION X-ray crystallization conditions：pH 6；pH 6	Resolution 3.04 Å R-free 0.217

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.

Other PDB	Difference from Current Entry 1LTR	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1B44 CRYSTAL STRUCTURE OF THE B SUBUNIT OF HEAT-LABILE ENTEROTOXIN FROM E. COLI CARRYING A PEPTIDE WITH ANTI-HSV ACTIVITY Deposited 1999-01-04	Different construct Different mutation/modification Different ligand/ion Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric	Chain D 22–124（103 aa） Fragment：SUBUNIT B Chain E 22–124（103 aa） Fragment：SUBUNIT B Chain F 22–124（103 aa） Fragment：SUBUNIT B Chain G 22–124（103 aa） Fragment：SUBUNIT B Chain H 22–124（103 aa） Fragment：SUBUNIT B	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions pH 6；pH 6	Resolution 3.30 Å R-free 0.255
2O2L Crystal structure of human heat-labile enterotoxin in complex with a blood group A antigen analog Deposited 2006-11-30	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Homooligomer；Protein × 5 PDB declaration: pentameric	Chain D 22–124（103 aa） Chain E 22–124（103 aa） Chain F 22–124（103 aa） Chain G 22–124（103 aa） Chain H 22–124（103 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.53 Å R-free 0.237
2O2L Crystal structure of human heat-labile enterotoxin in complex with a blood group A antigen analog Deposited 2006-11-30	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Other combination Homooligomer；Protein × 5 PDB declaration: pentameric	Chain I 22–124（103 aa） Chain J 22–124（103 aa） Chain K 22–124（103 aa） Chain L 22–124（103 aa） Chain M 22–124（103 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.53 Å R-free 0.237

2 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	ELBH_ECOLI
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain D； PDBConstruct 1–102； UniProt 22–123 Author chain E； PDBConstruct 1–102； UniProt 22–123 Author chain F； PDBConstruct 1–102； UniProt 22–123 Author chain G； PDBConstruct 1–102； UniProt 22–123 Author chain H； PDBConstruct 1–102； UniProt 22–123

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.

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	1ltr
Deposition date deposition_date	1998-07-31
Structure title title	CRYSTAL STRUCTURE OF THE B SUBUNIT OF HUMAN HEAT-LABILE ENTEROTOXIN FROM E. COLI CARRYING A PEPTIDE WITH ANTI-HSV ACTIVITY
Keywords keywords	B SUBUNIT, HEAT-LABILE ENTEROTOXIN, ANTI-HSV, ENTEROTOXIN; ENTEROTOXIN
Experimental Method method	X-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier	24.40 Å
Radius of gyration Rg (electron density) rg_electron	23.11 Å
Forward intensity I(0) i0	61541700.00
Molecular weight molecular_weight	60958.0 kDa
Excluded volume excluded_volume	76248 Å³
Envelope volume envelope_volume	88318 Å³
Hydration-shell volume shell_volume	30487 Å³
Envelope diameter envelope_diameter	74.1 Å
Shell Rg shell_rg	31.00 Å
Envelope Rg envelope_rg	23.05 Å
Shape Rg shape_rg	23.14 Å
Total Rg total_rg	23.84 Å
Total atoms total_atoms	4255
Residues n_residues	532
Spherical-harmonic order n_harmonics	20
q range q_range	— – 0.5000 Å⁻¹
Data points n_points	101
Shell type shell_type	directional
Solvent electron density solvent_density	0.3340 e/Å³
Shell contrast contrast_shell	0.0300 e/Å³
CRYSOL version crysol_version	4.1.3

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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax	71.9 Å
Rg (real space) rg_real	24.21 Å
Rg uncertainty (real space) rg_real_error	0.30 Å
I(0) (real space) i0_real	6.1540e+07
I(0) uncertainty (real space) i0_real_error	8.0900e+05
Rg (reciprocal space) rg_reciprocal	24.25 Å
I(0) (reciprocal space) i0_reciprocal	61540000.0000
Solution quality estimate total_estimate	0.9140
Solution quality rating solution_quality	EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	30.8 Å
Skewness Skewness skewness	0.080
Kurtosis Kurtosis kurtosis	-0.599
Angular range angular_range	— – 0.3250 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	24940000.0000
Real-space data points n_real_points	64
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.967; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.986; Smooth: 0.991

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (3)

Entity 1 Entity 1 polymer

Description description	HEAT-LABILE ENTEROTOXIN
Molecular weight formula_weight	12747.6 kDa
Mutation mutation	N103K
Source method src_method	man
Copy count entity_count	5

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	D,E,F,G,H
Atom count atom_count	4371

APQSITELCSEYHNTQIYTINDKILSYTESMAGKREMVIITFKSGATFQVEVPGSQHIDSQKKAIERMKDTLRITYLTETKIDKLCVWNNKTPNSIAAISMEKLYAGAVVNDL

来源 Source

来源生物 organism	Escherichia coli
NCBI Class编号 ncbi_taxonomy_id	562
宿主生物 host_organism	Vibrio sp.

Entity 2 Entity 2 non-polymer

Description description	SULFATE ION
Molecular weight formula_weight	96.1 kDa
Source method src_method	syn
Copy count entity_count	6

Entity 3 Entity 3 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	116

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7. Fold Classification (SCOP + CATH) 10 domains

SCOP 2.08 (5 domains)

Domain ID domain_id	d1ltrd_
Class class	b — All beta proteins
Fold Fold fold	b.40 — OB-fold
Superfamily Superfamily superfamily	b.40.2 — Bacterial enterotoxins
Family Family family	b.40.2.1 — Bacterial AB5 toxins, B-subunits

Domain ID domain_id	d1ltre_
Class class	b — All beta proteins
Fold Fold fold	b.40 — OB-fold
Superfamily Superfamily superfamily	b.40.2 — Bacterial enterotoxins
Family Family family	b.40.2.1 — Bacterial AB5 toxins, B-subunits

Domain ID domain_id	d1ltrf_
Class class	b — All beta proteins
Fold Fold fold	b.40 — OB-fold
Superfamily Superfamily superfamily	b.40.2 — Bacterial enterotoxins
Family Family family	b.40.2.1 — Bacterial AB5 toxins, B-subunits

Domain ID domain_id	d1ltrg_
Class class	b — All beta proteins
Fold Fold fold	b.40 — OB-fold
Superfamily Superfamily superfamily	b.40.2 — Bacterial enterotoxins
Family Family family	b.40.2.1 — Bacterial AB5 toxins, B-subunits

Domain ID domain_id	d1ltrh_
Class class	b — All beta proteins
Fold Fold fold	b.40 — OB-fold
Superfamily Superfamily superfamily	b.40.2 — Bacterial enterotoxins
Family Family family	b.40.2.1 — Bacterial AB5 toxins, B-subunits

CATH v4.4 (5 domains)

Domain ID domain_id	1ltrD00
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily	110 —

Domain ID domain_id	1ltrE00
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily	110 —

Domain ID domain_id	1ltrF00
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily	110 —

Domain ID domain_id	1ltrG00
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily	110 —

Domain ID domain_id	1ltrH00
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily	110 —

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8. Citations (3)

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Unit-cell length a length_a	127.230 Å
Unit-cell length b length_b	127.230 Å
Unit-cell length c length_c	174.190 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	40

Space group space_group	P 41 21 2
Space-group number int_tables_number	92
Crystal system crystal_system	—

Resolution resolution	3.040 Å
Low-resolution limit resolution_low	8.000 Å
R factor r_factor	0.1828
R_work r_work	0.1828
R_free r_free	0.2170

fit	/app/data/saxs_computation/lt/1ltr/1ltr.fit
pddf	/app/data/pr_computation/lt/1ltr/1ltr.pr.out
profile	/app/data/saxs_computation/lt/1ltr/1ltr.dat

CRYSTAL STRUCTURE OF THE B SUBUNIT OF HUMAN HEAT-LABILE ENTEROTOXIN FROM E. COLI CARRYING A PEPTIDE WITH ANTI-HSV ACTIVITY

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

HEAT-LABILE ENTEROTOXIN

State in the Current Structure

Other States of the Same Protein in the Database

SAXS scattering curve SAXS Profile

P(r) Distance Distribution P(r) Distribution

2. Structure Basics 2. Structure Basics

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

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

5. Crystallography and Experiment 5. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction