1cav

THE THREE-DIMENSIONAL STRUCTURE OF CANAVALIN FROM JACK BEAN (CANAVALIA ENSIFORMIS)

Method: X-RAY DIFFRACTION Dmax: 94.4 Å Quality: GOOD

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

CANAVALIN

Canavalia ensiformis

UniProt P50477

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 homooligomer Homooligomer Protein × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain A; UniProt 44–224 Chain B; UniProt 241–424 Not recorded No other associated polymer X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 2.60 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.

10 other PDB entries and 10 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CANA_CANEN
Isoform
PDB entities 1, 2
Chains and sequence ranges Author chain A; PDBConstruct 1–181; UniProt 44–224 Author chain B; PDBConstruct 1–184; UniProt 241–424

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 1cav

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1cav
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id1cav
Deposition date deposition_date1993-05-27
Structure title titleTHE THREE-DIMENSIONAL STRUCTURE OF CANAVALIN FROM JACK BEAN (CANAVALIA ENSIFORMIS)
Keywords keywordsSEED STORAGE PROTEIN; SEED STORAGE PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier25.18
Radius of gyration Rg (electron density) rg_electron24.29
Forward intensity I(0) i029676200.00
Molecular weight molecular_weight41521.0 kDa
Excluded volume excluded_volume51945 ų
Envelope volume envelope_volume66110 ų
Hydration-shell volume shell_volume24100 ų
Envelope diameter envelope_diameter97.0
Shell Rg shell_rg29.81
Envelope Rg envelope_rg24.98
Shape Rg shape_rg24.30
Total Rg total_rg24.91
Total atoms total_atoms2930
Residues n_residues365
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 dmax94.4
Rg (real space) rg_real25.35
Rg uncertainty (real space) rg_real_error1.00
I(0) (real space) i0_real2.9680e+07
I(0) uncertainty (real space) i0_real_error5.1040e+05
Rg (reciprocal space) rg_reciprocal25.30
I(0) (reciprocal space) i0_reciprocal29680000.0000
Solution quality estimate total_estimate0.7916
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary28.5
Skewness Skewness skewness0.664
Kurtosis Kurtosis kurtosis0.435
Angular range angular_range— – 0.3150 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha2831000.0000
Real-space data points n_real_points64
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.519; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.777; Smooth: 0.952

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1cava_
Class classb — All beta proteins
Fold Fold foldb.82 — Double-stranded beta-helix
Superfamily Superfamily superfamilyb.82.1 — RmlC-like cupins
Family Family familyb.82.1.2 — Germin/Seed storage 7S protein
Domain ID domain_idd1cavb_
Class classb — All beta proteins
Fold Fold foldb.82 — Double-stranded beta-helix
Superfamily Superfamily superfamilyb.82.1 — RmlC-like cupins
Family Family familyb.82.1.2 — Germin/Seed storage 7S protein

CATH v4.4 (2 domains)

Domain ID domain_id1cavA00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology120 — Jelly Rolls
Homologous superfamily homologous superfamily10 — Jelly Rolls
Domain ID domain_id1cavB00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology120 — Jelly Rolls
Homologous superfamily homologous superfamily10 — Jelly Rolls

8. Citations (2)

9. Files and Curves (10)