7yu4

Human Lysophosphatidic Acid Receptor 1-Gi complex bound to ONO-0740556, focused on receptor

Method: ELECTRON MICROSCOPY Dmax: 65.5 Å Quality: GOOD

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

Lysophosphatidic acid receptor 1

Homo sapiens

UniProt Q92633

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 2–364 Not recorded K6L [(2~{R})-2-[5-(2-hexylphenyl)pentanoylamino]-3-oxidanyl-propyl] dihydrogen phosphate × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.70 Å

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.

15 other PDB entries and 15 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name LPAR1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 11–373; UniProt 2–364

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 7yu4

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7yu4
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id7yu4
Deposition date deposition_date2022-08-16
Structure title titleHuman Lysophosphatidic Acid Receptor 1-Gi complex bound to ONO-0740556, focused on receptor
Keywords keywordsGPCR, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier20.29
Radius of gyration Rg (electron density) rg_electron19.18
Forward intensity I(0) i012741000.00
Molecular weight molecular_weight29148.0 kDa
Excluded volume excluded_volume37502 ų
Envelope volume envelope_volume43193 ų
Hydration-shell volume shell_volume19032 ų
Envelope diameter envelope_diameter65.1
Shell Rg shell_rg25.45
Envelope Rg envelope_rg19.64
Shape Rg shape_rg19.19
Total Rg total_rg20.18
Total atoms total_atoms2050
Residues n_residues266
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 dmax65.5
Rg (real space) rg_real20.30
Rg uncertainty (real space) rg_real_error0.44
I(0) (real space) i0_real1.2740e+07
I(0) uncertainty (real space) i0_real_error1.7350e+05
Rg (reciprocal space) rg_reciprocal20.30
I(0) (reciprocal space) i0_reciprocal12740000.0000
Solution quality estimate total_estimate0.8852
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary23.4
Skewness Skewness skewness0.375
Kurtosis Kurtosis kurtosis-0.356
Angular range angular_range— – 0.3900 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha2524000.0000
Real-space data points n_real_points71
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.862; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.994; Smooth: 0.926

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id7yu4A01
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology1070 — Rhopdopsin 7-helix transmembrane proteins
Homologous superfamily homologous superfamily10 — Rhodopsin 7-helix transmembrane proteins

8. Citations (1)

9. Files and Curves (10)