6e6p

HRAS G13D bound to GppNHp (Ha,b,c13GNP)

Method: X-RAY DIFFRACTION Dmax: 90.2 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:residues 1-166 Mutation:G13D GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER × 1 MG MAGNESIUM ION × 1 CA CALCIUM ION × 1 GOL GLYCEROL × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;291.15 K;152 mM Calcium Acetate, 22.8% PEG 3350, 9.5% stabilization buffer (20 mM HEPES pH 7.5, 50 mM NaCl, 20 mM MgCl2), Crystals were grown in 2uL by 2 uL drops of mother liquor to protein (22 mg/mL), Cryoprotectant: 70% glycerol and 30% mother liquor Resolution 1.93 Å R-free 0.237
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 1–166 Fragment:residues 1-166 Mutation:G13D GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER × 1 MG MAGNESIUM ION × 1 GOL GLYCEROL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;291.15 K;152 mM Calcium Acetate, 22.8% PEG 3350, 9.5% stabilization buffer (20 mM HEPES pH 7.5, 50 mM NaCl, 20 mM MgCl2), Crystals were grown in 2uL by 2 uL drops of mother liquor to protein (22 mg/mL), Cryoprotectant: 70% glycerol and 30% mother liquor Resolution 1.93 Å R-free 0.237
3 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain C; UniProt 1–166 Fragment:residues 1-166 Mutation:G13D GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER × 1 MG MAGNESIUM ION × 1 CA CALCIUM ION × 1 GOL GLYCEROL × 1 NA SODIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;291.15 K;152 mM Calcium Acetate, 22.8% PEG 3350, 9.5% stabilization buffer (20 mM HEPES pH 7.5, 50 mM NaCl, 20 mM MgCl2), Crystals were grown in 2uL by 2 uL drops of mother liquor to protein (22 mg/mL), Cryoprotectant: 70% glycerol and 30% mother liquor Resolution 1.93 Å R-free 0.237

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 B; PDBConstruct 1–166; UniProt 1–166 Author chain C; 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 6e6p

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6e6p
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6e6p
Deposition date deposition_date2018-07-25
Structure title titleHRAS G13D bound to GppNHp (Ha,b,c13GNP)
Keywords keywordsOncogene, RAS, p21, 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_guinier27.68
Radius of gyration Rg (electron density) rg_electron27.09
Forward intensity I(0) i054954200.00
Molecular weight molecular_weight55082.0 kDa
Excluded volume excluded_volume67686 ų
Envelope volume envelope_volume82880 ų
Hydration-shell volume shell_volume26563 ų
Envelope diameter envelope_diameter90.8
Shell Rg shell_rg33.23
Envelope Rg envelope_rg27.00
Shape Rg shape_rg27.09
Total Rg total_rg27.69
Total atoms total_atoms3848
Residues n_residues483
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 dmax90.2
Rg (real space) rg_real27.77
Rg uncertainty (real space) rg_real_error0.73
I(0) (real space) i0_real5.4950e+07
I(0) uncertainty (real space) i0_real_error8.2610e+05
Rg (reciprocal space) rg_reciprocal27.75
I(0) (reciprocal space) i0_reciprocal54950000.0000
Solution quality estimate total_estimate0.8860
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary26.9
Skewness Skewness skewness0.356
Kurtosis Kurtosis kurtosis-0.562
Angular range angular_range— – 0.2850 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha9608000.0000
Real-space data points n_real_points58
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.892; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.923; Smooth: 0.915

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

7. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (3 domains)

Domain ID domain_idd6e6pa_
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_idd6e6pb_
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_idd6e6pc_
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_id6e6pA00
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_id6e6pB00
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_id6e6pC00
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)