1lie

X-RAY CRYSTALLOGRAPHIC STRUCTURES OF ADIPOCYTE LIPID BINDING PROTEIN COMPLEXED WITH PALMITATE AND HEXADECANESULFONIC ACID. PROPERTIES OF CAVITY BINDING SITES

Method: X-RAY DIFFRACTION Dmax: 47.1 Å Quality: REASONABLE

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

ADIPOCYTE LIPID-BINDING PROTEIN

Mus musculus

UniProt P04117

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 1–131 Non-standard monomer:Yes (specific site not provided by mmCIF) PLM PALMITIC ACID × 2 PPI PROPANOIC ACID × 2 X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 1.60 Å R-free 0.239

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.

22 other PDB entries and 25 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name FABPA_MOUSE
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–131; UniProt 1–131

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 1lie

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1lie
Deposition date deposition_date1993-12-21
Structure title titleX-RAY CRYSTALLOGRAPHIC STRUCTURES OF ADIPOCYTE LIPID BINDING PROTEIN COMPLEXED WITH PALMITATE AND HEXADECANESULFONIC ACID. PROPERTIES OF CAVITY BINDING SITES
Keywords keywordsLIPID-BINDING PROTEIN, LIPID BINDING PROTEIN; LIPID BINDING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier15.20
Radius of gyration Rg (electron density) rg_electron13.90
Forward intensity I(0) i04282240.00
Molecular weight molecular_weight14884.0 kDa
Excluded volume excluded_volume18798 ų
Envelope volume envelope_volume21070 ų
Hydration-shell volume shell_volume12797 ų
Envelope diameter envelope_diameter45.6
Shell Rg shell_rg19.78
Envelope Rg envelope_rg14.06
Shape Rg shape_rg13.89
Total Rg total_rg15.16
Total atoms total_atoms1042
Residues n_residues130
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 dmax47.1
Rg (real space) rg_real15.06
Rg uncertainty (real space) rg_real_error0.19
I(0) (real space) i0_real4.2820e+06
I(0) uncertainty (real space) i0_real_error4.3750e+04
Rg (reciprocal space) rg_reciprocal15.07
I(0) (reciprocal space) i0_reciprocal4282000.0000
Solution quality estimate total_estimate0.7482
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary19.7
Skewness Skewness skewness0.057
Kurtosis Kurtosis kurtosis-0.415
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha934000.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.881; Stabil: 1.000; Sysdev: 0.368; Positv: 1.000; Valcen: 0.984; Smooth: 0.992

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_idd1liea_
Class classb — All beta proteins
Fold Fold foldb.60 — Lipocalins
Superfamily Superfamily superfamilyb.60.1 — Lipocalins
Family Family familyb.60.1.2 — Fatty acid binding protein-like

CATH v4.4 (1 domains)

Domain ID domain_id1lieA00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology128 — Lipocalin
Homologous superfamily homologous superfamily20 — Calycin beta-barrel core domain

8. Citations (1)

9. Files and Curves (10)