4imv

Ricin A-chain variant 1-33/44-198 with engineered disulfide bond, R48C/T77C/D75N

Method: X-RAY DIFFRACTION Dmax: 52.0 Å Quality: GOOD

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

Ricin

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 36–233 Fragment:unp residues 36-233 Mutation:R48C, T77C, D75N SO4 SULFATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.4;290 K;0.17 M Ammonium Sulfate, 25.5% (w/v) Peg 4000, 15% Glycerol , pH 6.4, VAPOR DIFFUSION, HANGING DROP, temperature 290K Resolution 2.25 Å R-free 0.242

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 2–189; UniProt 36–233

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 4imv

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4imv
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4imv
Deposition date deposition_date2013-01-03
Structure title titleRicin A-chain variant 1-33/44-198 with engineered disulfide bond, R48C/T77C/D75N
Keywords keywordsRicin, immunogen, vaccine, thermal stable, Ribosome Inactivating Protein (RIP), Hydrolase; HYDROLASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier16.65
Radius of gyration Rg (electron density) rg_electron15.11
Forward intensity I(0) i06639220.00
Molecular weight molecular_weight18737.0 kDa
Excluded volume excluded_volume23434 ų
Envelope volume envelope_volume26230 ų
Hydration-shell volume shell_volume14542 ų
Envelope diameter envelope_diameter51.6
Shell Rg shell_rg21.12
Envelope Rg envelope_rg15.31
Shape Rg shape_rg15.09
Total Rg total_rg16.27
Total atoms total_atoms1322
Residues n_residues168
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 dmax52.0
Rg (real space) rg_real16.48
Rg uncertainty (real space) rg_real_error0.23
I(0) (real space) i0_real6.6390e+06
I(0) uncertainty (real space) i0_real_error7.0710e+04
Rg (reciprocal space) rg_reciprocal16.50
I(0) (reciprocal space) i0_reciprocal6639000.0000
Solution quality estimate total_estimate0.8904
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary23.0
Skewness Skewness skewness0.004
Kurtosis Kurtosis kurtosis-0.475
Angular range angular_range— – 0.4800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1102000.0000
Real-space data points n_real_points78
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.865; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.980; Smooth: 0.998

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id4imvA00
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology420 — Ricin (A subunit); domain 1
Homologous superfamily homologous superfamily10 — Ricin (A subunit), domain 1

8. Citations (1)

9. Files and Curves (10)