1fk5

STRUCTURAL BASIS OF NON-SPECIFIC LIPID BINDING IN MAIZE LIPID-TRANSFER PROTEIN COMPLEXES WITH OLEIC ACID REVEALED BY HIGH-RESOLUTION X-RAY CRYSTALLOGRAPHY

Method: X-RAY DIFFRACTION Dmax: 42.6 Å Quality: GOOD

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

NONSPECIFIC LIPID-TRANSFER PROTEIN

OrganismNot specified

UniProt P19656

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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 28–120 Not recorded OLA OLEIC ACID × 1 FMT FORMIC ACID × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;298 K;3.6-4.8M Na formate, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K Resolution 1.30 Å R-free 0.188

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 10 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NLTP_MAIZE
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–93; UniProt 28–120

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 1fk5

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1fk5
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id1fk5
Deposition date deposition_date2000-08-09
Structure title titleSTRUCTURAL BASIS OF NON-SPECIFIC LIPID BINDING IN MAIZE LIPID-TRANSFER PROTEIN COMPLEXES WITH OLEIC ACID REVEALED BY HIGH-RESOLUTION X-RAY CRYSTALLOGRAPHY
Keywords keywordsprotein-lipid complex, LIPID TRANSPORT; LIPID TRANSPORT
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier13.64
Radius of gyration Rg (electron density) rg_electron12.12
Forward intensity I(0) i02266150.00
Molecular weight molecular_weight9481.0 kDa
Excluded volume excluded_volume11512 ų
Envelope volume envelope_volume12794 ų
Hydration-shell volume shell_volume9350 ų
Envelope diameter envelope_diameter39.3
Shell Rg shell_rg17.40
Envelope Rg envelope_rg12.18
Shape Rg shape_rg12.14
Total Rg total_rg13.25
Total atoms total_atoms655
Residues n_residues93
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 dmax42.6
Rg (real space) rg_real13.54
Rg uncertainty (real space) rg_real_error0.32
I(0) (real space) i0_real2.2660e+06
I(0) uncertainty (real space) i0_real_error2.5070e+04
Rg (reciprocal space) rg_reciprocal13.55
I(0) (reciprocal space) i0_reciprocal2266000.0000
Solution quality estimate total_estimate0.8921
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary18.9
Skewness Skewness skewness0.052
Kurtosis Kurtosis kurtosis-0.396
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha188700.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.870; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.995; Smooth: 0.990

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1fk5a_
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_id1fk5A00
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)