1uva

Lipid Binding in Rice Nonspecific Lipid Transfer Protein-1 Complexes from Oryza sativa

Method: X-RAY DIFFRACTION Dmax: 40.3 Å Quality: GOOD

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

NONSPECIFIC LIPID TRANSFER PROTEIN 1

OrganismNot specified

UniProt P23096

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 26–116 Not recorded MYR MYRISTIC ACID × 2 X-RAY DIFFRACTION X-ray crystallization conditions:pH 5.6;POLYETHYLENE GLYCOL 600, pH 5.60 Resolution 2.50 Å R-free 0.288

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.

4 other PDB entries and 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NLT1_ORYSA
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–91; UniProt 26–116

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 1uva

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1uva
Deposition date deposition_date2004-01-19
Structure title titleLipid Binding in Rice Nonspecific Lipid Transfer Protein-1 Complexes from Oryza sativa
Keywords keywordsLIPID TRANSPORT, LTP 1, PAP 1, RICE, FATTY ACID BINDING; LIPID TRANSPORT
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier13.40
Radius of gyration Rg (electron density) rg_electron11.95
Forward intensity I(0) i02038760.00
Molecular weight molecular_weight9146.0 kDa
Excluded volume excluded_volume11237 ų
Envelope volume envelope_volume12556 ų
Hydration-shell volume shell_volume9275 ų
Envelope diameter envelope_diameter39.3
Shell Rg shell_rg17.16
Envelope Rg envelope_rg12.04
Shape Rg shape_rg11.96
Total Rg total_rg13.15
Total atoms total_atoms632
Residues n_residues91
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 dmax40.3
Rg (real space) rg_real13.30
Rg uncertainty (real space) rg_real_error0.24
I(0) (real space) i0_real2.0390e+06
I(0) uncertainty (real space) i0_real_error1.9130e+04
Rg (reciprocal space) rg_reciprocal13.30
I(0) (reciprocal space) i0_reciprocal2039000.0000
Solution quality estimate total_estimate0.8160
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary18.9
Skewness Skewness skewness-0.001
Kurtosis Kurtosis kurtosis-0.374
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha179400.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.875; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.981; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1uvaa_
Class classa — All alpha proteins
Fold Fold folda.52 — Bifunctional inhibitor/lipid-transfer protein/seed storage 2S albumin
Superfamily Superfamily superfamilya.52.1 — Bifunctional inhibitor/lipid-transfer protein/seed storage 2S albumin
Family Family familya.52.1.1 — Plant lipid-transfer and hydrophobic proteins

CATH v4.4 (1 domains)

Domain ID domain_id1uvaA00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology110 — Hydrophobic Seed Protein
Homologous superfamily homologous superfamily10 — Plant lipid-transfer and hydrophobic proteins

8. Citations (1)

9. Files and Curves (10)