1loe

X-RAY CRYSTAL STRUCTURE DETERMINATION AND REFINEMENT AT 1.9 ANGSTROMS RESOLUTION OF ISOLECTIN I FROM THE SEEDS OF LATHYRUS OCHRUS

Method: X-RAY DIFFRACTION Dmax: 84.2 Å Quality: GOOD

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

LEGUME ISOLECTIN I (ALPHA CHAIN)

Lathyrus ochrus

UniProt P04122

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 heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 1–181 Chain C; UniProt 1–181 Not recorded LEGUME ISOLECTIN I (BETA CHAIN) × 2 (P12306) CA CALCIUM ION × 2 MN MANGANESE (II) ION × 2 X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 1.90 Å
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 1–181 Not recorded LEGUME ISOLECTIN I (BETA CHAIN) × 1 (P12306) CA CALCIUM ION × 1 MN MANGANESE (II) ION × 1 X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 1.90 Å
3 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 1–181 Not recorded LEGUME ISOLECTIN I (BETA CHAIN) × 1 (P12306) CA CALCIUM ION × 1 MN MANGANESE (II) ION × 1 X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 1.90 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.

8 other PDB entries and 26 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name LECB_LATOC
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–181; UniProt 1–181 Author chain C; PDBConstruct 1–181; UniProt 1–181

LEGUME ISOLECTIN I (BETA CHAIN)

Lathyrus ochrus

UniProt P12306

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 heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain B; UniProt 1–52 Chain D; UniProt 1–52 Not recorded LEGUME ISOLECTIN I (ALPHA CHAIN) × 2 (P04122) CA CALCIUM ION × 2 MN MANGANESE (II) ION × 2 X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 1.90 Å
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain D; UniProt 1–52 Not recorded LEGUME ISOLECTIN I (ALPHA CHAIN) × 1 (P04122) CA CALCIUM ION × 1 MN MANGANESE (II) ION × 1 X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 1.90 Å
3 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 1–52 Not recorded LEGUME ISOLECTIN I (ALPHA CHAIN) × 1 (P04122) CA CALCIUM ION × 1 MN MANGANESE (II) ION × 1 X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 1.90 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.

6 other PDB entries and 22 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name LEC1_LATOC
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–52; UniProt 1–52 Author chain D; PDBConstruct 1–52; UniProt 1–52

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 1loe

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1loe
Deposition date deposition_date1993-01-27
Structure title titleX-RAY CRYSTAL STRUCTURE DETERMINATION AND REFINEMENT AT 1.9 ANGSTROMS RESOLUTION OF ISOLECTIN I FROM THE SEEDS OF LATHYRUS OCHRUS
Keywords keywordsLECTIN; LECTIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier25.73
Radius of gyration Rg (electron density) rg_electron24.75
Forward intensity I(0) i040556600.00
Molecular weight molecular_weight50267.0 kDa
Excluded volume excluded_volume63089 ų
Envelope volume envelope_volume72284 ų
Hydration-shell volume shell_volume25102 ų
Envelope diameter envelope_diameter88.2
Shell Rg shell_rg31.24
Envelope Rg envelope_rg24.96
Shape Rg shape_rg24.72
Total Rg total_rg25.60
Total atoms total_atoms3560
Residues n_residues454
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 dmax84.2
Rg (real space) rg_real25.85
Rg uncertainty (real space) rg_real_error0.60
I(0) (real space) i0_real4.0560e+07
I(0) uncertainty (real space) i0_real_error5.7760e+05
Rg (reciprocal space) rg_reciprocal25.81
I(0) (reciprocal space) i0_reciprocal40560000.0000
Solution quality estimate total_estimate0.8754
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary25.8
Skewness Skewness skewness0.460
Kurtosis Kurtosis kurtosis-0.395
Angular range angular_range— – 0.3100 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha6766000.0000
Real-space data points n_real_points63
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.838; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.943; Smooth: 0.918

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1loe.1
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_idd1loe.2
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 (2 domains)

Domain ID domain_id1loeA00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology120 — Jelly Rolls
Homologous superfamily homologous superfamily200
Domain ID domain_id1loeC00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology120 — Jelly Rolls
Homologous superfamily homologous superfamily200

8. Citations (1)

9. Files and Curves (10)