6v7l

The structure of the P212121 crystal form of canavalin at 173 K

Method: X-RAY DIFFRACTION Dmax: 107.7 Å Quality: EXCELLENT

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 1–445 Chain B; UniProt 1–445 Chain C; UniProt 1–445 Not recorded BEZ BENZOIC ACID × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.5;298 K;Crystals were grown by sitting drop vapor diffusion from 18% PEG 3350 in 0.1 M HEPES reservoirs. The drops were equal amounts of a 40 mg/ml solution of precanavalin (not treated with any exogenous protease) in water. Crystals grew only after six to eight weeks at room temperature. Resolution 2.80 Å R-free 0.252

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
Chains and sequence ranges Author chain A; PDBConstruct 1–445; UniProt 1–445 Author chain B; PDBConstruct 1–445; UniProt 1–445 Author chain C; PDBConstruct 1–445; UniProt 1–445

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 6v7l

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6v7l
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6v7l
Deposition date deposition_date2019-12-08
Structure title titleThe structure of the P212121 crystal form of canavalin at 173 K
Keywords keywordsprecanavalin, proteolytic cleavage, plant protein, vicillim, storage protein, benzoic acid; PLANT PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier34.07
Radius of gyration Rg (electron density) rg_electron32.85
Forward intensity I(0) i0218446000.00
Molecular weight molecular_weight119440.0 kDa
Excluded volume excluded_volume149800 ų
Envelope volume envelope_volume186700 ų
Hydration-shell volume shell_volume46343 ų
Envelope diameter envelope_diameter106.1
Shell Rg shell_rg40.70
Envelope Rg envelope_rg32.54
Shape Rg shape_rg32.84
Total Rg total_rg33.47
Total atoms total_atoms16779
Residues n_residues1046
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 dmax107.7
Rg (real space) rg_real33.97
Rg uncertainty (real space) rg_real_error0.55
I(0) (real space) i0_real2.1840e+08
I(0) uncertainty (real space) i0_real_error2.6480e+06
Rg (reciprocal space) rg_reciprocal34.03
I(0) (reciprocal space) i0_reciprocal218500000.0000
Solution quality estimate total_estimate0.9081
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary37.5
Skewness Skewness skewness0.180
Kurtosis Kurtosis kurtosis-0.672
Angular range angular_range— – 0.2300 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha162900000.0000
Real-space data points n_real_points47
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.937; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.989

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (6 domains)

Domain ID domain_idd6v7la1
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_idd6v7la2
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_idd6v7lb1
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_idd6v7lb2
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_idd6v7lc1
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_idd6v7lc2
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

8. Citations (1)

9. Files and Curves (10)