4lgr

Ricin A chain bound to camelid nanobody (VHH3)

Method: X-RAY DIFFRACTION Dmax: 91.8 Å Quality: REASONABLE

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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 40–294 Fragment:UNP residues 40-294 Camelid nanobody (VHH3) × 1 ZN ZINC ION × 3 ACY ACETIC ACID × 2 CL CHLORIDE ION × 8 EDO 1,2-ETHANEDIOL × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 4.5;293 K;100 mM NaAcetate, 200 mM Zinc Acetate, 10% PEG 3000, pH 4.5, VAPOR DIFFUSION, temperature 293K Resolution 1.65 Å R-free 0.204

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 1–255; UniProt 40–294

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 4lgr

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id4lgr
Deposition date deposition_date2013-06-28
Structure title titleRicin A chain bound to camelid nanobody (VHH3)
Keywords keywordsRibosome inhibiting protein 2, HYDROLASE-IMMUNE SYSTEM complex; HYDROLASE/IMMUNE SYSTEM
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier24.89
Radius of gyration Rg (electron density) rg_electron23.98
Forward intensity I(0) i032242300.00
Molecular weight molecular_weight42169.0 kDa
Excluded volume excluded_volume52074 ų
Envelope volume envelope_volume62434 ų
Hydration-shell volume shell_volume23001 ų
Envelope diameter envelope_diameter100.9
Shell Rg shell_rg29.75
Envelope Rg envelope_rg24.56
Shape Rg shape_rg23.88
Total Rg total_rg24.93
Total atoms total_atoms2951
Residues n_residues375
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 dmax91.8
Rg (real space) rg_real25.09
Rg uncertainty (real space) rg_real_error1.08
I(0) (real space) i0_real3.2240e+07
I(0) uncertainty (real space) i0_real_error5.7510e+05
Rg (reciprocal space) rg_reciprocal25.04
I(0) (reciprocal space) i0_reciprocal32240000.0000
Solution quality estimate total_estimate0.7260
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary26.2
Skewness Skewness skewness0.570
Kurtosis Kurtosis kurtosis0.037
Angular range angular_range— – 0.3200 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha6487000.0000
Real-space data points n_real_points64
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.582; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.689; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

7. Fold Classification (SCOP + CATH) 5 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd4lgra_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.165 — Ribosome inactivating proteins (RIP)
Superfamily Superfamily superfamilyd.165.1 — Ribosome inactivating proteins (RIP)
Family Family familyd.165.1.1 — Plant cytotoxins
Domain ID domain_idd4lgrb_
Class classb — All beta proteins
Fold Fold foldb.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamilyb.1.1 — Immunoglobulin
Family Family familyb.1.1.1 — V set domains (antibody variable domain-like)

CATH v4.4 (3 domains)

Domain ID domain_id4lgrA01
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
Domain ID domain_id4lgrA02
Class class4 — Few Secondary Structures
Architecture architecture10 — Irregular
Topology topology470 — Ricin (A Subunit), domain 2
Homologous superfamily homologous superfamily10 — Ricin (A Subunit), domain 2
Domain ID domain_id4lgrB00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins

8. Citations (1)

9. Files and Curves (10)