2aai

Crystallographic refinement of ricin to 2.5 Angstroms

Method: X-RAY DIFFRACTION Dmax: 84.4 Å Quality: REASONABLE

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 Other combination Homooligomer Protein × 2 其他Polymer 4 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 36–302 Chain B; UniProt 315–576 Not recorded beta-D-galactopyranose-(1-4)-beta-D-glucopyranose × 2 ;alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose ; × 2 X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 2.50 Å

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 2aai

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2aai
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2aai
Deposition date deposition_date1993-09-07
Structure title titleCrystallographic refinement of ricin to 2.5 Angstroms
Keywords keywordsGLYCOSIDASE, HYDROLASE; HYDROLASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier26.46
Radius of gyration Rg (electron density) rg_electron25.47
Forward intensity I(0) i063708200.00
Molecular weight molecular_weight61358.0 kDa
Excluded volume excluded_volume76415 ų
Envelope volume envelope_volume92008 ų
Hydration-shell volume shell_volume30305 ų
Envelope diameter envelope_diameter88.0
Shell Rg shell_rg32.64
Envelope Rg envelope_rg25.44
Shape Rg shape_rg25.47
Total Rg total_rg26.21
Total atoms total_atoms4317
Residues n_residues529
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 dmax84.4
Rg (real space) rg_real26.43
Rg uncertainty (real space) rg_real_error0.54
I(0) (real space) i0_real6.3710e+07
I(0) uncertainty (real space) i0_real_error8.1440e+05
Rg (reciprocal space) rg_reciprocal26.44
I(0) (reciprocal space) i0_reciprocal63710000.0000
Solution quality estimate total_estimate0.7364
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary29.6
Skewness Skewness skewness0.323
Kurtosis Kurtosis kurtosis-0.401
Angular range angular_range— – 0.3000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha12210000.0000
Real-space data points n_real_points61
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.911; Stabil: 1.000; Sysdev: 0.291; Positv: 1.000; Valcen: 0.997; Smooth: 0.968

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 7 domains

SCOP 2.08 (3 domains)

Domain ID domain_idd2aaia_
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_idd2aaib1
Class classb — All beta proteins
Fold Fold foldb.42 — beta-Trefoil
Superfamily Superfamily superfamilyb.42.2 — Ricin B-like lectins
Family Family familyb.42.2.1 — Ricin B-like
Domain ID domain_idd2aaib2
Class classb — All beta proteins
Fold Fold foldb.42 — beta-Trefoil
Superfamily Superfamily superfamilyb.42.2 — Ricin B-like lectins
Family Family familyb.42.2.1 — Ricin B-like

CATH v4.4 (4 domains)

Domain ID domain_id2aaiA01
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_id2aaiA02
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_id2aaiB01
Class class2 — Mainly Beta
Architecture architecture80 — Trefoil
Topology topology10 — Trefoil (Acidic Fibroblast Growth Factor, subunit A)
Homologous superfamily homologous superfamily50
Domain ID domain_id2aaiB02
Class class2 — Mainly Beta
Architecture architecture80 — Trefoil
Topology topology10 — Trefoil (Acidic Fibroblast Growth Factor, subunit A)
Homologous superfamily homologous superfamily50

8. Citations (4)

9. Files and Curves (10)