9e42

RTA-RUNT-192 complex

Method: X-RAY DIFFRACTION Dmax: 103.5 Å Quality: REASONABLE

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

Ricin A chain

Ricinus communis

UniProt P02879

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 36–302 Fragment:residues 40-294 A1BH2 5-(2,6-diethylphenyl)thiophene-2-carboxylic acid × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;295 K;170 mM diammonium hydrogen phosphate Resolution 1.80 Å R-free 0.246
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 36–302 Fragment:residues 40-294 A1BH2 5-(2,6-diethylphenyl)thiophene-2-carboxylic acid × 1 EDO 1,2-ETHANEDIOL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;295 K;170 mM diammonium hydrogen phosphate Resolution 1.80 Å R-free 0.246

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.

100 other PDB entries and 125 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RICI_RICCO
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 5–271; UniProt 36–302 Author chain B; PDBConstruct 5–271; UniProt 36–302

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 9e42

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9e42
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9e42
Deposition date deposition_date2024-10-24
最后修订 last_revision2025-05-14
Structure title titleRTA-RUNT-192 complex
Keywords keywordsN-linked glycosidase, TOXIN, HYDROLASE-INHIBITOR complex; TOXIN,HYDROLASE/INHIBITOR
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier27.36
Radius of gyration Rg (electron density) rg_electron26.99
Forward intensity I(0) i0103665000.00
Molecular weight molecular_weight53810.0 kDa
Excluded volume excluded_volume52047 ų
Envelope volume envelope_volume87215 ų
Hydration-shell volume shell_volume27848 ų
Envelope diameter envelope_diameter94.6
Shell Rg shell_rg33.49
Envelope Rg envelope_rg27.06
Shape Rg shape_rg26.99
Total Rg total_rg27.48
Total atoms total_atoms4092
Residues n_residues509
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 dmax103.5
Rg (real space) rg_real27.52
Rg uncertainty (real space) rg_real_error1.30
I(0) (real space) i0_real1.0370e+08
I(0) uncertainty (real space) i0_real_error1.6240e+06
Rg (reciprocal space) rg_reciprocal27.47
I(0) (reciprocal space) i0_reciprocal103700000.0000
Solution quality estimate total_estimate0.7153
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary28.5
Skewness Skewness skewness0.496
Kurtosis Kurtosis kurtosis-0.325
Angular range angular_range— – 0.2900 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha17840000.0000
Real-space data points n_real_points59
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.527; Stabil: 0.995; Sysdev: 1.000; Positv: 1.000; Valcen: 0.727; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)