1as2

GDP+PI BOUND G42V GIA1

Method: X-RAY DIFFRACTION Dmax: 70.8 Å Quality: GOOD

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

GIA1

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 1–353 Mutation:G42V PO4 PHOSPHATE ION × 1 GDP GUANOSINE-5'-DIPHOSPHATE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.6;THE PROTEIN WAS CRYSTALLIZED IN HANGING DROPS USING 3M (NH4)H2P04 AS THE PRECIPITANT (PH 5.6). 50 MM HEPES, PH 8.0, 10 MM MGSO4, 10 MM DTT AND 5 MM GDP WAS THE BUFFER, vapor diffusion - hanging drop Resolution 2.80 Å R-free 0.250

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 1–353; UniProt 1–353

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 1as2

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1as2
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1as2
Deposition date deposition_date1997-08-11
Structure title titleGDP+PI BOUND G42V GIA1
Keywords keywordsSIGNAL TRANSDUCTION, GTPASE; SIGNAL TRANSDUCTION
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier21.64
Radius of gyration Rg (electron density) rg_electron20.82
Forward intensity I(0) i023431800.00
Molecular weight molecular_weight36635.0 kDa
Excluded volume excluded_volume45731 ų
Envelope volume envelope_volume53859 ų
Hydration-shell volume shell_volume21783 ų
Envelope diameter envelope_diameter71.2
Shell Rg shell_rg27.35
Envelope Rg envelope_rg21.02
Shape Rg shape_rg20.84
Total Rg total_rg21.63
Total atoms total_atoms2571
Residues n_residues315
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 dmax70.8
Rg (real space) rg_real21.61
Rg uncertainty (real space) rg_real_error0.38
I(0) (real space) i0_real2.3430e+07
I(0) uncertainty (real space) i0_real_error2.8160e+05
Rg (reciprocal space) rg_reciprocal21.62
I(0) (reciprocal space) i0_reciprocal23430000.0000
Solution quality estimate total_estimate0.8893
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary25.4
Skewness Skewness skewness0.348
Kurtosis Kurtosis kurtosis-0.259
Angular range angular_range— – 0.3650 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha4614000.0000
Real-space data points n_real_points68
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.856; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.992; Smooth: 0.998

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1as2a1
Class classa — All alpha proteins
Fold Fold folda.66 — Transducin (alpha subunit), insertion domain
Superfamily Superfamily superfamilya.66.1 — Transducin (alpha subunit), insertion domain
Family Family familya.66.1.1 — Transducin (alpha subunit), insertion domain
Domain ID domain_idd1as2a2
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.37 — P-loop containing nucleoside triphosphate hydrolases
Superfamily Superfamily superfamilyc.37.1 — P-loop containing nucleoside triphosphate hydrolases
Family Family familyc.37.1.8 — G proteins

CATH v4.4 (2 domains)

Domain ID domain_id1as2A01
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_id1as2A02
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)