3qe0

A Galpha-i1 P-loop mutation prevents transition to the activated state

Method: X-RAY DIFFRACTION Dmax: 119.0 Å Quality: GOOD

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

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 33–354 Fragment:alpha-i1 subunit, residues 33-354 Mutation:G42R KB752 peptide × 1 MG MAGNESIUM ION × 1 GDP GUANOSINE-5'-DIPHOSPHATE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;291 K;Hanging drops were a 1:1 mixture of protein-peptide complex in buffer (50 mM HEPES pH 8.0, 10 mM magnesium chloride, 10 microM GppNHp, 1 mM EDTA, 5 mM DTT) and well solution (17% (w/v) PEG MME 5K, 200 mM magnesium chloride, 100 mM HEPES pH 7.0), VAPOR DIFFUSION, HANGING DROP, temperature 291K Resolution 3.00 Å R-free 0.292
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 33–354 Fragment:alpha-i1 subunit, residues 33-354 Mutation:G42R KB752 peptide × 1 MG MAGNESIUM ION × 1 GDP GUANOSINE-5'-DIPHOSPHATE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;291 K;Hanging drops were a 1:1 mixture of protein-peptide complex in buffer (50 mM HEPES pH 8.0, 10 mM magnesium chloride, 10 microM GppNHp, 1 mM EDTA, 5 mM DTT) and well solution (17% (w/v) PEG MME 5K, 200 mM magnesium chloride, 100 mM HEPES pH 7.0), VAPOR DIFFUSION, HANGING DROP, temperature 291K Resolution 3.00 Å R-free 0.292
3 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain C; UniProt 33–354 Fragment:alpha-i1 subunit, residues 33-354 Mutation:G42R MG MAGNESIUM ION × 1 GDP GUANOSINE-5'-DIPHOSPHATE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;291 K;Hanging drops were a 1:1 mixture of protein-peptide complex in buffer (50 mM HEPES pH 8.0, 10 mM magnesium chloride, 10 microM GppNHp, 1 mM EDTA, 5 mM DTT) and well solution (17% (w/v) PEG MME 5K, 200 mM magnesium chloride, 100 mM HEPES pH 7.0), VAPOR DIFFUSION, HANGING DROP, temperature 291K Resolution 3.00 Å R-free 0.292

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 589 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GNAI1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 4–325; UniProt 33–354 Author chain B; PDBConstruct 4–325; UniProt 33–354 Author chain C; PDBConstruct 4–325; UniProt 33–354

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 3qe0

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3qe0
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3qe0
Deposition date deposition_date2011-01-19
Structure title titleA Galpha-i1 P-loop mutation prevents transition to the activated state
Keywords keywords;KB752, Ras-like domain, all-helical domain, arginine finger, signaling protein, lipoprotein, transducer, GTPase activity, GTP binding, nucleotide binding, ADP-ribosylation ;; SIGNALING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier37.24
Radius of gyration Rg (electron density) rg_electron36.72
Forward intensity I(0) i0184983000.00
Molecular weight molecular_weight109920.0 kDa
Excluded volume excluded_volume137590 ų
Envelope volume envelope_volume181030 ų
Hydration-shell volume shell_volume41751 ų
Envelope diameter envelope_diameter118.0
Shell Rg shell_rg41.79
Envelope Rg envelope_rg36.36
Shape Rg shape_rg36.72
Total Rg total_rg37.08
Total atoms total_atoms7718
Residues n_residues944
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 dmax119.0
Rg (real space) rg_real37.16
Rg uncertainty (real space) rg_real_error1.06
I(0) (real space) i0_real1.8500e+08
I(0) uncertainty (real space) i0_real_error3.1500e+06
Rg (reciprocal space) rg_reciprocal37.22
I(0) (reciprocal space) i0_reciprocal185000000.0000
Solution quality estimate total_estimate0.8321
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary51.0
Skewness Skewness skewness0.129
Kurtosis Kurtosis kurtosis-0.725
Angular range angular_range— – 0.2100 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha26110000.0000
Real-space data points n_real_points43
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.940; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.993; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 6 domains

CATH v4.4 (6 domains)

Domain ID domain_id3qe0A01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily300 — P-loop containing nucleotide triphosphate hydrolases
Domain ID domain_id3qe0A02
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology400 — GI Alpha 1, domain 2-like
Homologous superfamily homologous superfamily10 — GI Alpha 1, domain 2-like
Domain ID domain_id3qe0B01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily300 — P-loop containing nucleotide triphosphate hydrolases
Domain ID domain_id3qe0B02
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology400 — GI Alpha 1, domain 2-like
Homologous superfamily homologous superfamily10 — GI Alpha 1, domain 2-like
Domain ID domain_id3qe0C01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily300 — P-loop containing nucleotide triphosphate hydrolases
Domain ID domain_id3qe0C02
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology400 — GI Alpha 1, domain 2-like
Homologous superfamily homologous superfamily10 — GI Alpha 1, domain 2-like

8. Citations (2)

9. Files and Curves (10)