4lgs

Ricin A chain bound to camelid nanobody (VHH4)

Method: X-RAY DIFFRACTION Dmax: 87.0 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 39–301 Fragment:UNP residues 39-301 Camelid nanobody (VHH4) × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 7.5;293 K;100 mM NaHepes, 20% PEG 8000, pH 7.5, VAPOR DIFFUSION, temperature 293K Resolution 2.70 Å R-free 0.248

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 1–263; UniProt 39–301

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 4lgs

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id4lgs
Deposition date deposition_date2013-06-28
Structure title titleRicin A chain bound to camelid nanobody (VHH4)
Keywords keywordsRibosomal 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_guinier25.37
Radius of gyration Rg (electron density) rg_electron24.67
Forward intensity I(0) i032568100.00
Molecular weight molecular_weight43235.0 kDa
Excluded volume excluded_volume53826 ų
Envelope volume envelope_volume64822 ų
Hydration-shell volume shell_volume23346 ų
Envelope diameter envelope_diameter91.1
Shell Rg shell_rg30.13
Envelope Rg envelope_rg24.98
Shape Rg shape_rg24.63
Total Rg total_rg25.44
Total atoms total_atoms3052
Residues n_residues392
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 dmax87.0
Rg (real space) rg_real25.51
Rg uncertainty (real space) rg_real_error0.64
I(0) (real space) i0_real3.2570e+07
I(0) uncertainty (real space) i0_real_error4.3480e+05
Rg (reciprocal space) rg_reciprocal25.47
I(0) (reciprocal space) i0_reciprocal32570000.0000
Solution quality estimate total_estimate0.6494
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary26.2
Skewness Skewness skewness0.522
Kurtosis Kurtosis kurtosis-0.205
Angular range angular_range— – 0.3150 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha6019000.0000
Real-space data points n_real_points64
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.780; Stabil: 1.000; Sysdev: 0.120; Positv: 1.000; Valcen: 0.806; Smooth: 0.931

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 5 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd4lgsa_
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_idd4lgsb_
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_id4lgsA01
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_id4lgsA02
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_id4lgsB00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins

8. Citations (1)

9. Files and Curves (10)