1axy

ERYTHRINA CORALLODENDRON LECTIN

Method: X-RAY DIFFRACTION Dmax: 65.4 Å Quality: REASONABLE

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

LECTIN

OrganismNot specified

UniProt P16404

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 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 27–265 Not recorded ;beta-D-xylopyranose-(1-2)-[alpha-D-mannopyranose-(1-3)][alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-3)]2-acetamido-2-deoxy-beta-D-glucopyranose ; × 2 MN MANGANESE (II) ION × 2 CA CALCIUM ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:pH 7;pH 7. Resolution 1.95 Å R-free 0.200

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 13 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name LEC_ERYCO
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–239; UniProt 27–265

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 1axy

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1axy
Deposition date deposition_date1997-10-24
Structure title titleERYTHRINA CORALLODENDRON LECTIN
Keywords keywordsLECTIN, GLYCOPROTEIN; LECTIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier19.00
Radius of gyration Rg (electron density) rg_electron17.74
Forward intensity I(0) i013152600.00
Molecular weight molecular_weight27466.0 kDa
Excluded volume excluded_volume34431 ų
Envelope volume envelope_volume39367 ų
Hydration-shell volume shell_volume18490 ų
Envelope diameter envelope_diameter65.2
Shell Rg shell_rg24.13
Envelope Rg envelope_rg18.20
Shape Rg shape_rg17.68
Total Rg total_rg18.88
Total atoms total_atoms1937
Residues n_residues239
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 dmax65.4
Rg (real space) rg_real18.92
Rg uncertainty (real space) rg_real_error0.40
I(0) (real space) i0_real1.3150e+07
I(0) uncertainty (real space) i0_real_error1.4780e+05
Rg (reciprocal space) rg_reciprocal18.93
I(0) (reciprocal space) i0_reciprocal13150000.0000
Solution quality estimate total_estimate0.6851
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary24.5
Skewness Skewness skewness0.256
Kurtosis Kurtosis kurtosis-0.207
Angular range angular_range— – 0.4200 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha2944000.0000
Real-space data points n_real_points73
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.730; Stabil: 1.000; Sysdev: 0.242; Positv: 1.000; Valcen: 0.996; Smooth: 0.988

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1axya_
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 (1 domains)

Domain ID domain_id1axyA00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology120 — Jelly Rolls
Homologous superfamily homologous superfamily200

8. Citations (1)

9. Files and Curves (10)