1cq9

PEANUT LECTIN-TRICLINIC FORM

Method: X-RAY DIFFRACTION Dmax: 91.6 Å Quality: EXCELLENT

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

PROTEIN (PEANUT LECTIN)

OrganismNot specified

UniProt P02872

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 1–236 Chain B; UniProt 1–236 Chain C; UniProt 1–236 Chain D; UniProt 1–236 Not recorded CA CALCIUM ION × 4 MN MANGANESE (II) ION × 4 X-RAY DIFFRACTION X-ray crystallization conditions:pH 4.6;pH 4.6 Resolution 3.50 Å R-free 0.278

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.

25 other PDB entries and 29 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name LECG_ARAHY
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–236; UniProt 1–236 Author chain B; PDBConstruct 1–236; UniProt 1–236 Author chain C; PDBConstruct 1–236; UniProt 1–236 Author chain D; PDBConstruct 1–236; UniProt 1–236

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 1cq9

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1cq9
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1cq9
Deposition date deposition_date1999-08-06
Structure title titlePEANUT LECTIN-TRICLINIC FORM
Keywords keywordsLECTIN, LEGUME LECTIN, OPEN QUATERNARY STRUCTURE, TRICLINIC FORM, ACIDIC PH; LECTIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier30.53
Radius of gyration Rg (electron density) rg_electron29.27
Forward intensity I(0) i0155255000.00
Molecular weight molecular_weight99034.0 kDa
Excluded volume excluded_volume123810 ų
Envelope volume envelope_volume150110 ų
Hydration-shell volume shell_volume41673 ų
Envelope diameter envelope_diameter93.4
Shell Rg shell_rg37.51
Envelope Rg envelope_rg28.97
Shape Rg shape_rg29.24
Total Rg total_rg30.09
Total atoms total_atoms6980
Residues n_residues928
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 dmax91.6
Rg (real space) rg_real30.33
Rg uncertainty (real space) rg_real_error0.38
I(0) (real space) i0_real1.5530e+08
I(0) uncertainty (real space) i0_real_error1.9230e+06
Rg (reciprocal space) rg_reciprocal30.41
I(0) (reciprocal space) i0_reciprocal155300000.0000
Solution quality estimate total_estimate0.9093
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary40.5
Skewness Skewness skewness0.060
Kurtosis Kurtosis kurtosis-0.614
Angular range angular_range— – 0.2600 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha25280000.0000
Real-space data points n_real_points53
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.964; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.989; Smooth: 0.935

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (4 domains)

Domain ID domain_idd1cq9a_
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_idd1cq9b_
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_idd1cq9c_
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_idd1cq9d_
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_id1cq9A00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology120 — Jelly Rolls
Homologous superfamily homologous superfamily200
Domain ID domain_id1cq9B00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology120 — Jelly Rolls
Homologous superfamily homologous superfamily200
Domain ID domain_id1cq9C00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology120 — Jelly Rolls
Homologous superfamily homologous superfamily200
Domain ID domain_id1cq9D00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology120 — Jelly Rolls
Homologous superfamily homologous superfamily200

8. Citations (5)

9. Files and Curves (10)