8bos

Transition state analogue complex of small G protein and its GAP effector

Method: X-RAY DIFFRACTION Dmax: 94.3 Å Quality: REASONABLE

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

GTPase HRas

Homo sapiens

UniProt P01112

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 R; UniProt 1–166 Fragment:GTPase HRAS N-terminally processed Ras GTPase-activating protein 1 × 1 (P20936) GDP GUANOSINE-5'-DIPHOSPHATE × 1 MGF TRIFLUOROMAGNESATE × 1 MG MAGNESIUM ION × 1 GAI GUANIDINE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8;293 K;precipitant: HEPES-Na 100 mM pH = 8.0, PEG3350 22% (w/v), (NH4)2SO4 20 mM, Gd-HCl 100 mM, NaF 20 mM protein buffer: HRas 0.400 mM, RasGAP 0.400 mM, HEPES-Na 20 mM, NaF 20 mM drop size: 5 uL, protein:precipitant ratio: 1:1.2 Resolution 2.10 Å R-free 0.280

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.

242 other PDB entries and 324 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RASH_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain R; PDBConstruct 1–166; UniProt 1–166

Ras GTPase-activating protein 1

Homo sapiens

UniProt P20936

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 G; UniProt 713–1042 Not recorded GTPase HRas × 1 (P01112) GDP GUANOSINE-5'-DIPHOSPHATE × 1 MGF TRIFLUOROMAGNESATE × 1 MG MAGNESIUM ION × 1 GAI GUANIDINE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8;293 K;precipitant: HEPES-Na 100 mM pH = 8.0, PEG3350 22% (w/v), (NH4)2SO4 20 mM, Gd-HCl 100 mM, NaF 20 mM protein buffer: HRas 0.400 mM, RasGAP 0.400 mM, HEPES-Na 20 mM, NaF 20 mM drop size: 5 uL, protein:precipitant ratio: 1:1.2 Resolution 2.10 Å R-free 0.280

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.

14 other PDB entries and 26 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RASA1_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain G; PDBConstruct 2–331; UniProt 713–1042

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 8bos

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8bos
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8bos
Deposition date deposition_date2022-11-15
Structure title titleTransition state analogue complex of small G protein and its GAP effector
Keywords keywordstransition state analogue complex, metal fluoride complex, Ras, signalling protein, RasGAP, oncoprotein, HYDROLASE; HYDROLASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier24.96
Radius of gyration Rg (electron density) rg_electron24.01
Forward intensity I(0) i052020500.00
Molecular weight molecular_weight55903.0 kDa
Excluded volume excluded_volume69991 ų
Envelope volume envelope_volume82796 ų
Hydration-shell volume shell_volume28517 ų
Envelope diameter envelope_diameter84.5
Shell Rg shell_rg31.37
Envelope Rg envelope_rg24.30
Shape Rg shape_rg24.02
Total Rg total_rg24.80
Total atoms total_atoms3915
Residues n_residues486
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 dmax94.3
Rg (real space) rg_real24.88
Rg uncertainty (real space) rg_real_error0.79
I(0) (real space) i0_real5.2020e+07
I(0) uncertainty (real space) i0_real_error7.5510e+05
Rg (reciprocal space) rg_reciprocal24.90
I(0) (reciprocal space) i0_reciprocal52020000.0000
Solution quality estimate total_estimate0.7411
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary28.4
Skewness Skewness skewness0.295
Kurtosis Kurtosis kurtosis-0.323
Angular range angular_range— – 0.3200 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha11060000.0000
Real-space data points n_real_points64
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.590; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.861; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

8. Citations (1)

9. Files and Curves (10)