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1mid

Non-specific lipid transfer protein 1 from barley in complex with L-alfa-lysophosphatidylcholine, Laudoyl

Method: X-RAY DIFFRACTION Dmax: 41.6 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

nonspecific lipid-transfer protein 1

OrganismNot specified

UniProt P07597

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 27–117 Not recorded LAP [2-((1-OXODODECANOXY-(2-HYDROXY-3-PROPANYL))-PHOSPHONATE-OXY)-ETHYL]-TRIMETHYLAMMONIUM × 3 X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 8.5；298 K；1.1M sodium citrate, 0.1M Tris, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K Resolution 1.71 Å R-free 0.212

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.

Other PDB Difference from Current Entry 1MID Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1BE2 LIPID TRANSFER PROTEIN COMPLEXED WITH PALMITATE, NMR, 10 STRUCTURES Deposited 1998-05-19 Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 27–117（91 aa）
Not recorded PLM PALMITIC ACID × 1 SOLUTION NMR
NMR measurement conditions pH 7.2；310 K
Resolution not provided
1JTB LIPID TRANSFER PROTEIN COMPLEXED WITH PALMITOYL COENZYME A, NMR, 16 STRUCTURES Deposited 1996-12-03 Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 27–117（91 aa）
Not recorded COA COENZYME A × 1 PLM PALMITIC ACID × 1 SOLUTION NMR
NMR measurement conditions pH 7.2；310 K
Resolution not provided
1LIP BARLEY LIPID TRANSFER PROTEIN (NMR, 4 STRUCTURES) Deposited 1995-09-21 Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 27–117（91 aa）
Not recorded No recorded non-water small molecule SOLUTION NMR mmCIF provides none of the parsed conditions Resolution not provided
3GSH Three-dimensional structure of a post translational modified barley LTP1 Deposited 2009-03-27 Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 27–117（91 aa）
Not recorded ZN ZINC ION × 3 NA SODIUM ION × 2 TFA trifluoroacetic acid × 1 ASY (12E)-10-oxooctadec-12-enoic acid × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；300 K；0.1M CACODYLATE BUFFER PH6.5, 16% PEG 8000, 0.23M ZINC ACETATE , VAPOR DIFFUSION, HANGING DROP, temperature 300K
Resolution 1.80 Å R-free 0.262
3GSH Three-dimensional structure of a post translational modified barley LTP1 Deposited 2009-03-27 Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 27–117（91 aa）
Not recorded ZN ZINC ION × 1 NA SODIUM ION × 1 TFA trifluoroacetic acid × 1 ASY (12E)-10-oxooctadec-12-enoic acid × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；300 K；0.1M CACODYLATE BUFFER PH6.5, 16% PEG 8000, 0.23M ZINC ACETATE , VAPOR DIFFUSION, HANGING DROP, temperature 300K
Resolution 1.80 Å R-free 0.262

4 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NLTP1_HORVU
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–91； UniProt 27–117

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 1mid

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1mid
Deposition date deposition_date2002-08-23
Structure title titleNon-specific lipid transfer protein 1 from barley in complex with L-alfa-lysophosphatidylcholine, Laudoyl
Keywords keywordslipid transfer, LIPID BINDING PROTEIN; LIPID BINDING PROTEIN
Experimental Method methodX-RAY DIFFRACTION
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier13.63 Å
Radius of gyration Rg (electron density) rg_electron11.94 Å
Forward intensity I(0) i02274850.00
Molecular weight molecular_weight9943.0 kDa
Excluded volume excluded_volume12260 ų
Envelope volume envelope_volume13206 ų
Hydration-shell volume shell_volume9602 ų
Envelope diameter envelope_diameter41.2 Å
Shell Rg shell_rg17.43 Å
Envelope Rg envelope_rg12.19 Å
Shape Rg shape_rg11.99 Å
Total Rg total_rg13.07 Å
Total atoms total_atoms690
Residues n_residues91
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−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
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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax41.6 Å
Rg (real space) rg_real13.52 Å
Rg uncertainty (real space) rg_real_error0.21 Å
I(0) (real space) i0_real2.2750e+06
I(0) uncertainty (real space) i0_real_error2.3000e+04
Rg (reciprocal space) rg_reciprocal13.53 Å
I(0) (reciprocal space) i0_reciprocal2275000.0000
Solution quality estimate total_estimate0.8139
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary41.1 Å
Skewness Skewness skewness0.016
Kurtosis Kurtosis kurtosis-0.351
Angular range angular_range— – 0.5000 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha210500.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.865; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.984; Smooth: 0.000
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (3)

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7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1mida_
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_id1midA00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology110 — Hydrophobic Seed Protein
Homologous superfamily homologous superfamily10 — Plant lipid-transfer and hydrophobic proteins
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8. Citations (1)

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9. Files and Curves (10)