7kdu

Ricin bound to VHH antibody V5E4

Method: X-RAY DIFFRACTION Dmax: 86.5 Å Quality: EXCELLENT

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

Ricin chain A

OrganismNot specified

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 Other combination Heteromer Protein × 3 其他Polymer 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 36–302 Chain B; UniProt 315–576 Not recorded VHH antibody V5E4 × 1 alpha-L-fucopyranose-(1-3)-2-acetamido-2-deoxy-beta-D-glucopyranose × 1 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 2 EDO 1,2-ETHANEDIOL × 1 ZN ZINC ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;293 K;290 mM zinc Aaetate and 17% PEG 3,350 Resolution 2.81 Å R-free 0.294

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, 2
Chains and sequence ranges Author chain A; PDBConstruct 1–267; UniProt 36–302 Author chain B; PDBConstruct 1–262; UniProt 315–576

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 7kdu

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7kdu
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7kdu
Deposition date deposition_date2020-10-09
Structure title titleRicin bound to VHH antibody V5E4
Keywords keywordsRibosome inactivating protein, TOXIN; TOXIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier27.99
Radius of gyration Rg (electron density) rg_electron26.92
Forward intensity I(0) i081065500.00
Molecular weight molecular_weight69374.0 kDa
Excluded volume excluded_volume86225 ų
Envelope volume envelope_volume104000 ų
Hydration-shell volume shell_volume32319 ų
Envelope diameter envelope_diameter88.3
Shell Rg shell_rg34.31
Envelope Rg envelope_rg27.13
Shape Rg shape_rg26.92
Total Rg total_rg27.65
Total atoms total_atoms4878
Residues n_residues611
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 dmax86.5
Rg (real space) rg_real27.91
Rg uncertainty (real space) rg_real_error0.48
I(0) (real space) i0_real8.1070e+07
I(0) uncertainty (real space) i0_real_error1.1130e+06
Rg (reciprocal space) rg_reciprocal27.94
I(0) (reciprocal space) i0_reciprocal81070000.0000
Solution quality estimate total_estimate0.9079
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary30.3
Skewness Skewness skewness0.224
Kurtosis Kurtosis kurtosis-0.612
Angular range angular_range— – 0.2850 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha19850000.0000
Real-space data points n_real_points58
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.959; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.923

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (8)

7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id7kduC01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins

8. Citations (1)

9. Files and Curves (10)