4pam

A conserved phenylalanine as relay between the 5 helix and the GDP binding region of heterotrimeric G protein

Method: X-RAY DIFFRACTION Dmax: 83.2 Å Quality: REASONABLE

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

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

Rattus norvegicus

UniProt P10824

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 1–354 Mutation:F336C GDP GUANOSINE-5'-DIPHOSPHATE × 1 SO3 SULFITE ION × 1 CL CHLORIDE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;291 K;(NH4)2SO3, Sodium acetate Resolution 2.10 Å R-free 0.218

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.

43 other PDB entries and 57 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GNAI1_RAT
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–354; UniProt 1–354

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 4pam

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4pam
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4pam
Deposition date deposition_date2014-04-09
Structure title titleA conserved phenylalanine as relay between the 5 helix and the GDP binding region of heterotrimeric G protein
Keywords keywordsActivation of Heterotrimeric G protein, GDP release, Computer modeling, G protein Coupled Receptors, Rhodopsin, SIGNALING PROTEIN; SIGNALING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier23.31
Radius of gyration Rg (electron density) rg_electron22.48
Forward intensity I(0) i026668600.00
Molecular weight molecular_weight38774.0 kDa
Excluded volume excluded_volume48248 ų
Envelope volume envelope_volume58090 ų
Hydration-shell volume shell_volume22315 ų
Envelope diameter envelope_diameter85.6
Shell Rg shell_rg28.74
Envelope Rg envelope_rg22.87
Shape Rg shape_rg22.48
Total Rg total_rg23.26
Total atoms total_atoms2715
Residues n_residues337
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 dmax83.2
Rg (real space) rg_real23.39
Rg uncertainty (real space) rg_real_error0.61
I(0) (real space) i0_real2.6670e+07
I(0) uncertainty (real space) i0_real_error3.7610e+05
Rg (reciprocal space) rg_reciprocal23.37
I(0) (reciprocal space) i0_reciprocal26670000.0000
Solution quality estimate total_estimate0.6414
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary25.6
Skewness Skewness skewness0.479
Kurtosis Kurtosis kurtosis-0.100
Angular range angular_range— – 0.3400 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha5402000.0000
Real-space data points n_real_points66
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.717; Stabil: 1.000; Sysdev: 0.115; Positv: 1.000; Valcen: 0.896; Smooth: 0.942

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 2 domains

CATH v4.4 (2 domains)

Domain ID domain_id4pamA01
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_id4pamA02
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 (1)

9. Files and Curves (10)