7l0q

Structure of NTS-NTSR1-Gi complex in lipid nanodisc, canonical state, with AHD

Method: ELECTRON MICROSCOPY Dmax: 122.7 Å Quality: GOOD

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

Neurotensin receptor type 1

Rattus norvegicus

UniProt P20789

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 heterocomplex Heteromer Protein × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain C; UniProt 50–390 Mutation:A86L, H103D, H105Y, A161V, R213L, V234L, I253A, H305R, F358V, S362A, del273-290 Neurotensin × 1 (P20068) Guanine nucleotide-binding protein G(i) subunit alpha-1 × 1 (P63096) Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1 × 1 (P62873) Guanine nucleotide-binding protein G(T) subunit gamma-T1 × 1 (P63211) ELECTRON MICROSCOPY cryo-EM buffer:pH 6.9 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.30 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.

24 other PDB entries and 28 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NTR1_RAT
Isoform
PDB entities 1
Chains and sequence ranges Author chain C; PDBConstruct 5–327; UniProt 50–390

Neurotensin

Rattus norvegicus

UniProt P20068

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 heterocomplex Heteromer Protein × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain D; UniProt 157–162 Fragment:residues 157-162 Neurotensin receptor type 1 × 1 (P20789) Guanine nucleotide-binding protein G(i) subunit alpha-1 × 1 (P63096) Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1 × 1 (P62873) Guanine nucleotide-binding protein G(T) subunit gamma-T1 × 1 (P63211) ELECTRON MICROSCOPY cryo-EM buffer:pH 6.9 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.30 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.

12 other PDB entries and 16 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NEUT_RAT
Isoform
PDB entities 2
Chains and sequence ranges Author chain D; PDBConstruct 5–10; UniProt 157–162

Guanine nucleotide-binding protein G(i) subunit alpha-1

Homo sapiens

UniProt P63096

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 heterocomplex Heteromer Protein × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain A; UniProt 1–354 Not recorded Neurotensin receptor type 1 × 1 (P20789) Neurotensin × 1 (P20068) Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1 × 1 (P62873) Guanine nucleotide-binding protein G(T) subunit gamma-T1 × 1 (P63211) ELECTRON MICROSCOPY cryo-EM buffer:pH 6.9 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.30 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.

573 other PDB entries and 591 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GNAI1_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain A; PDBConstruct 1–354; UniProt 1–354

Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1

Homo sapiens

UniProt P62873

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 heterocomplex Heteromer Protein × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain B; UniProt 2–340 Not recorded Neurotensin receptor type 1 × 1 (P20789) Neurotensin × 1 (P20068) Guanine nucleotide-binding protein G(i) subunit alpha-1 × 1 (P63096) Guanine nucleotide-binding protein G(T) subunit gamma-T1 × 1 (P63211) ELECTRON MICROSCOPY cryo-EM buffer:pH 6.9 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.30 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.

1260 other PDB entries and 1263 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GBB1_HUMAN
Isoform
PDB entities 4
Chains and sequence ranges Author chain B; PDBConstruct 23–361; UniProt 2–340

Guanine nucleotide-binding protein G(T) subunit gamma-T1

Homo sapiens

UniProt P63211

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 heterocomplex Heteromer Protein × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain G; UniProt 2–74 Not recorded Neurotensin receptor type 1 × 1 (P20789) Neurotensin × 1 (P20068) Guanine nucleotide-binding protein G(i) subunit alpha-1 × 1 (P63096) Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1 × 1 (P62873) ELECTRON MICROSCOPY cryo-EM buffer:pH 6.9 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.30 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.

3 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GBG1_HUMAN
Isoform
PDB entities 5
Chains and sequence ranges Author chain G; PDBConstruct 11–83; UniProt 2–74

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 7l0q

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7l0q
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id7l0q
Deposition date deposition_date2020-12-12
Structure title titleStructure of NTS-NTSR1-Gi complex in lipid nanodisc, canonical state, with AHD
Keywords keywordsGPCR, NTSR1, NTS, G protein, Nanodisc, SIGNALING PROTEIN; SIGNALING PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier35.80
Radius of gyration Rg (electron density) rg_electron35.71
Forward intensity I(0) i0189288000.00
Molecular weight molecular_weight111840.0 kDa
Excluded volume excluded_volume140490 ų
Envelope volume envelope_volume180770 ų
Hydration-shell volume shell_volume44179 ų
Envelope diameter envelope_diameter129.5
Shell Rg shell_rg39.96
Envelope Rg envelope_rg35.51
Shape Rg shape_rg35.73
Total Rg total_rg35.94
Total atoms total_atoms7856
Residues n_residues1002
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 dmax122.7
Rg (real space) rg_real35.92
Rg uncertainty (real space) rg_real_error1.05
I(0) (real space) i0_real1.8930e+08
I(0) uncertainty (real space) i0_real_error3.0980e+06
Rg (reciprocal space) rg_reciprocal35.85
I(0) (reciprocal space) i0_reciprocal189300000.0000
Solution quality estimate total_estimate0.8733
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary41.8
Skewness Skewness skewness0.439
Kurtosis Kurtosis kurtosis-0.205
Angular range angular_range— – 0.2200 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha43320000.0000
Real-space data points n_real_points45
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.839; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.929; Smooth: 0.904

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)