1azd

CONCANAVALIN FROM CANAVALIA BRASILIENSIS

Method: X-RAY DIFFRACTION Dmax: 85.0 Å Quality: EXCELLENT

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

CONBR

OrganismNot specified

UniProt P55915

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 1–237 Chain B; UniProt 1–237 Chain C; UniProt 1–237 Chain D; UniProt 1–237 Not recorded CA CALCIUM ION × 4 MN MANGANESE (II) ION × 4 X-RAY DIFFRACTION X-ray crystallization conditions:pH 6;2 MICRO-L CBR (10 MG/ML) 2 MICRO-L (11-15% PEG 6000, 0.1 M MES PH 6, pH 6.0 Resolution 3.00 Å R-free 0.240

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.

19 other PDB entries and 24 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CONA_CANBR
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–237; UniProt 1–237 Author chain B; PDBConstruct 1–237; UniProt 1–237 Author chain C; PDBConstruct 1–237; UniProt 1–237 Author chain D; PDBConstruct 1–237; UniProt 1–237

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 1azd

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1azd
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1azd
Deposition date deposition_date1997-11-16
Structure title titleCONCANAVALIN FROM CANAVALIA BRASILIENSIS
Keywords keywordsLEGUME LECTIN, LECTIN; LECTIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier30.08
Radius of gyration Rg (electron density) rg_electron28.69
Forward intensity I(0) i0167984000.00
Molecular weight molecular_weight102630.0 kDa
Excluded volume excluded_volume128060 ų
Envelope volume envelope_volume151480 ų
Hydration-shell volume shell_volume42892 ų
Envelope diameter envelope_diameter87.7
Shell Rg shell_rg37.05
Envelope Rg envelope_rg28.59
Shape Rg shape_rg28.65
Total Rg total_rg29.53
Total atoms total_atoms7236
Residues n_residues948
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 dmax85.0
Rg (real space) rg_real29.86
Rg uncertainty (real space) rg_real_error0.40
I(0) (real space) i0_real1.6800e+08
I(0) uncertainty (real space) i0_real_error2.4750e+06
Rg (reciprocal space) rg_reciprocal29.95
I(0) (reciprocal space) i0_reciprocal168000000.0000
Solution quality estimate total_estimate0.9038
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary38.5
Skewness Skewness skewness0.009
Kurtosis Kurtosis kurtosis-0.692
Angular range angular_range— – 0.2650 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha34540000.0000
Real-space data points n_real_points54
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.989; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.991; Smooth: 0.786

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (4 domains)

Domain ID domain_idd1azda_
Class classb — All beta proteins
Fold Fold foldb.29 — Concanavalin A-like lectins/glucanases
Superfamily Superfamily superfamilyb.29.1 — Concanavalin A-like lectins/glucanases
Family Family familyb.29.1.1 — Legume lectins
Domain ID domain_idd1azdb_
Class classb — All beta proteins
Fold Fold foldb.29 — Concanavalin A-like lectins/glucanases
Superfamily Superfamily superfamilyb.29.1 — Concanavalin A-like lectins/glucanases
Family Family familyb.29.1.1 — Legume lectins
Domain ID domain_idd1azdc_
Class classb — All beta proteins
Fold Fold foldb.29 — Concanavalin A-like lectins/glucanases
Superfamily Superfamily superfamilyb.29.1 — Concanavalin A-like lectins/glucanases
Family Family familyb.29.1.1 — Legume lectins
Domain ID domain_idd1azdd_
Class classb — All beta proteins
Fold Fold foldb.29 — Concanavalin A-like lectins/glucanases
Superfamily Superfamily superfamilyb.29.1 — Concanavalin A-like lectins/glucanases
Family Family familyb.29.1.1 — Legume lectins

CATH v4.4 (4 domains)

Domain ID domain_id1azdA00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology120 — Jelly Rolls
Homologous superfamily homologous superfamily200
Domain ID domain_id1azdB00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology120 — Jelly Rolls
Homologous superfamily homologous superfamily200
Domain ID domain_id1azdC00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology120 — Jelly Rolls
Homologous superfamily homologous superfamily200
Domain ID domain_id1azdD00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology120 — Jelly Rolls
Homologous superfamily homologous superfamily200

8. Citations (1)

9. Files and Curves (10)