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1jtb

LIPID TRANSFER PROTEIN COMPLEXED WITH PALMITOYL COENZYME A, NMR, 16 STRUCTURES

Method: SOLUTION NMR Dmax: 37.7 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

LIPID TRANSFER PROTEIN

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 COA COENZYME A × 1 PLM PALMITIC ACID × 1 SOLUTION NMR NMR measurement conditions：pH 7.2；310 K Resolution not provided

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 1JTB 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 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
1LIP BARLEY LIPID TRANSFER PROTEIN (NMR, 4 STRUCTURES) Deposited 1995-09-21 Different ligand/ion Different experimental conditions 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
1MID Non-specific lipid transfer protein 1 from barley in complex with L-alfa-lysophosphatidylcholine, Laudoyl Deposited 2002-08-23 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 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
3GSH Three-dimensional structure of a post translational modified barley LTP1 Deposited 2009-03-27 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 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 method 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 NLT1_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 1jtb

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1jtb
Deposition date deposition_date1996-12-03
Structure title titleLIPID TRANSFER PROTEIN COMPLEXED WITH PALMITOYL COENZYME A, NMR, 16 STRUCTURES
Keywords keywordsLIPID TRANSPORT, LIPID TRANSFER PROTEIN; LIPID TRANSPORT
Experimental Method methodSOLUTION NMR
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier12.47 Å
Radius of gyration Rg (electron density) rg_electron11.78 Å
Forward intensity I(0) i0515301000.00
Molecular weight molecular_weight171280.0 kDa
Excluded volume excluded_volume206480 ų
Envelope volume envelope_volume20637 ų
Hydration-shell volume shell_volume12773 ų
Envelope diameter envelope_diameter40.3 Å
Shell Rg shell_rg19.65 Å
Envelope Rg envelope_rg13.62 Å
Shape Rg shape_rg11.81 Å
Total Rg total_rg11.86 Å
Total atoms total_atoms23184
Residues n_residues1456
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 dmax37.7 Å
Rg (real space) rg_real12.32 Å
Rg uncertainty (real space) rg_real_error0.21 Å
I(0) (real space) i0_real5.1530e+08
I(0) uncertainty (real space) i0_real_error5.0130e+06
Rg (reciprocal space) rg_reciprocal12.33 Å
I(0) (reciprocal space) i0_reciprocal515300000.0000
Solution quality estimate total_estimate0.8800
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary18.6 Å
Skewness Skewness skewness-0.137
Kurtosis Kurtosis kurtosis-0.470
Angular range angular_range— – 0.5000 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha205300.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.831; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.972; Smooth: 0.972
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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_idd1jtba_
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_id1jtbA00
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 (3)

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9. Files and Curves (10)