8tab

RTA-PD00589

Method: X-RAY DIFFRACTION Dmax: 60.5 Å Quality: GOOD

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 39–296 Not recorded CL CHLORIDE ION × 3 U4T 4H,5H-naphtho[1,2-b]thiophene-2-carboxylic acid × 1 EDO 1,2-ETHANEDIOL × 2 2PE NONAETHYLENE GLYCOL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.5;295 K;200 mM Mg(NO3)2 and 20% PEG 3350 Resolution 2.26 Å R-free 0.219

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 126 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 1–258; UniProt 39–296

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 8tab

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8tab
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8tab
Deposition date deposition_date2023-06-27
Structure title titleRTA-PD00589
Keywords keywordsN-glycosidase, inhibitor, 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_guinier19.50
Radius of gyration Rg (electron density) rg_electron18.11
Forward intensity I(0) i015443600.00
Molecular weight molecular_weight29458.0 kDa
Excluded volume excluded_volume36815 ų
Envelope volume envelope_volume42612 ų
Hydration-shell volume shell_volume19393 ų
Envelope diameter envelope_diameter61.4
Shell Rg shell_rg24.63
Envelope Rg envelope_rg18.37
Shape Rg shape_rg18.11
Total Rg total_rg19.08
Total atoms total_atoms2075
Residues n_residues258
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 dmax60.5
Rg (real space) rg_real19.36
Rg uncertainty (real space) rg_real_error0.34
I(0) (real space) i0_real1.5440e+07
I(0) uncertainty (real space) i0_real_error2.0980e+05
Rg (reciprocal space) rg_reciprocal19.38
I(0) (reciprocal space) i0_reciprocal15440000.0000
Solution quality estimate total_estimate0.8161
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary25.6
Skewness Skewness skewness0.130
Kurtosis Kurtosis kurtosis-0.395
Angular range angular_range— – 0.4100 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha4065000.0000
Real-space data points n_real_points72
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.874; Stabil: 0.997; Sysdev: 1.000; Positv: 1.000; Valcen: 0.993; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

8. Citations (1)

9. Files and Curves (10)