1lri

BETA-CRYPTOGEIN-CHOLESTEROL COMPLEX

Method: X-RAY DIFFRACTION Dmax: 45.9 Å Quality: GOOD

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

Beta-elicitin cryptogein

OrganismNot specified

UniProt P15570

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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 21–118 Not recorded CL CHLORIDE ION × 1 CLR CHOLESTEROL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;290 K;sodium chloride, cholesterol, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 290K Resolution 1.45 Å R-free 0.188

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.

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

View Construct and Data Evidence
UniProt name ELIB_PHYCR
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–98; UniProt 21–118

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 1lri

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1lri
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1lri
Deposition date deposition_date2002-05-15
Structure title titleBETA-CRYPTOGEIN-CHOLESTEROL COMPLEX
Keywords keywordscryptogein, cholesterol, sterol carrier protein, TOXIN; TOXIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier14.03
Radius of gyration Rg (electron density) rg_electron12.55
Forward intensity I(0) i02312900.00
Molecular weight molecular_weight10746.0 kDa
Excluded volume excluded_volume13563 ų
Envelope volume envelope_volume14563 ų
Hydration-shell volume shell_volume10126 ų
Envelope diameter envelope_diameter43.8
Shell Rg shell_rg17.99
Envelope Rg envelope_rg12.75
Shape Rg shape_rg12.54
Total Rg total_rg13.85
Total atoms total_atoms745
Residues n_residues98
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 dmax45.9
Rg (real space) rg_real13.93
Rg uncertainty (real space) rg_real_error0.34
I(0) (real space) i0_real2.3130e+06
I(0) uncertainty (real space) i0_real_error2.8210e+04
Rg (reciprocal space) rg_reciprocal13.94
I(0) (reciprocal space) i0_reciprocal2313000.0000
Solution quality estimate total_estimate0.8764
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary19.8
Skewness Skewness skewness0.039
Kurtosis Kurtosis kurtosis-0.382
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha178400.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.805; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.974

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1lria_
Class classa — All alpha proteins
Fold Fold folda.134 — Fungal elicitin
Superfamily Superfamily superfamilya.134.1 — Fungal elicitin
Family Family familya.134.1.1 — Fungal elicitin

CATH v4.4 (1 domains)

Domain ID domain_id1lriA00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology239 — Beta-cryptogein
Homologous superfamily homologous superfamily10 — Elicitin domain

8. Citations (1)

9. Files and Curves (10)