3lo5

Crystal Structure of the dominant negative S17N mutant of Ras

Method: X-RAY DIFFRACTION Dmax: 89.3 Å Quality: GOOD

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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 1–166 Fragment:H-Ras (UNP residues 1-166) Mutation:S17N GDP GUANOSINE-5'-DIPHOSPHATE × 1 CA CALCIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;293 K;15% (v/v) PEG400, 13% (w/v) PEG8000, 0.2 M calcium acetate, and 0.1 M Tris-HCl pH = 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 2.57 Å R-free 0.296
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain C; UniProt 1–166 Fragment:H-Ras (UNP residues 1-166) Mutation:S17N GDP GUANOSINE-5'-DIPHOSPHATE × 1 CA CALCIUM ION × 1 SO4 SULFATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;293 K;15% (v/v) PEG400, 13% (w/v) PEG8000, 0.2 M calcium acetate, and 0.1 M Tris-HCl pH = 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 2.57 Å R-free 0.296
3 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain E; UniProt 1–166 Fragment:H-Ras (UNP residues 1-166) Mutation:S17N GDP GUANOSINE-5'-DIPHOSPHATE × 1 CA CALCIUM ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;293 K;15% (v/v) PEG400, 13% (w/v) PEG8000, 0.2 M calcium acetate, and 0.1 M Tris-HCl pH = 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 2.57 Å R-free 0.296

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 322 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 A; PDBConstruct 1–166; UniProt 1–166 Author chain C; PDBConstruct 1–166; UniProt 1–166 Author chain E; PDBConstruct 1–166; UniProt 1–166

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 3lo5

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3lo5
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3lo5
Deposition date deposition_date2010-02-03
Structure title titleCrystal Structure of the dominant negative S17N mutant of Ras
Keywords keywords;Ras, nucleotide exchange, dominant negative, Mg2+, Acetylation, Cell membrane, Disease mutation, Golgi apparatus, GTP-binding, Lipoprotein, Membrane, Methylation, Nucleotide-binding, Palmitate, Prenylation, Proto-oncogene, S-nitrosylation, ONCOPROTEIN ;; ONCOPROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier27.28
Radius of gyration Rg (electron density) rg_electron26.77
Forward intensity I(0) i047525700.00
Molecular weight molecular_weight51405.0 kDa
Excluded volume excluded_volume63365 ų
Envelope volume envelope_volume77002 ų
Hydration-shell volume shell_volume25105 ų
Envelope diameter envelope_diameter91.5
Shell Rg shell_rg32.62
Envelope Rg envelope_rg26.96
Shape Rg shape_rg26.73
Total Rg total_rg27.45
Total atoms total_atoms3592
Residues n_residues450
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 dmax89.3
Rg (real space) rg_real27.45
Rg uncertainty (real space) rg_real_error0.89
I(0) (real space) i0_real4.7530e+07
I(0) uncertainty (real space) i0_real_error7.8080e+05
Rg (reciprocal space) rg_reciprocal27.40
I(0) (reciprocal space) i0_reciprocal47520000.0000
Solution quality estimate total_estimate0.8707
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary26.2
Skewness Skewness skewness0.469
Kurtosis Kurtosis kurtosis-0.409
Angular range angular_range— – 0.2900 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha8885000.0000
Real-space data points n_real_points59
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.842; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.922; Smooth: 0.870

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (3 domains)

Domain ID domain_idd3lo5a_
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
Domain ID domain_idd3lo5c_
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
Domain ID domain_idd3lo5e_
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 (3 domains)

Domain ID domain_id3lo5A00
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_id3lo5C00
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_id3lo5E00
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily300 — P-loop containing nucleotide triphosphate hydrolases

8. Citations (1)

9. Files and Curves (10)