5wpl

KRas G12V, bound to GppNHp and miniprotein 225-11

Method: X-RAY DIFFRACTION Dmax: 144.6 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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 1–166 Fragment:residues 1-166 Ras-binding peptide × 2 GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER × 1 MG MAGNESIUM ION × 1 CA CALCIUM ION × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293 K;0.1 M ammonium sulfate and 20-25% PEG3,350 Resolution 2.15 Å R-free 0.258
2 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain D; UniProt 1–166 Fragment:residues 1-166 Ras-binding peptide × 2 GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER × 1 MG MAGNESIUM ION × 1 CA CALCIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293 K;0.1 M ammonium sulfate and 20-25% PEG3,350 Resolution 2.15 Å R-free 0.258
3 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain G; UniProt 1–166 Fragment:residues 1-166 Ras-binding peptide × 2 GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER × 1 MG MAGNESIUM ION × 2 CA CALCIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293 K;0.1 M ammonium sulfate and 20-25% PEG3,350 Resolution 2.15 Å R-free 0.258
4 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain J; UniProt 1–166 Fragment:residues 1-166 Ras-binding peptide × 2 GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER × 1 MG MAGNESIUM ION × 1 CA CALCIUM ION × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293 K;0.1 M ammonium sulfate and 20-25% PEG3,350 Resolution 2.15 Å R-free 0.258

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 321 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 D; PDBConstruct 1–166; UniProt 1–166 Author chain G; PDBConstruct 1–166; UniProt 1–166 Author chain J; 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 5wpl

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5wpl
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5wpl
Deposition date deposition_date2017-08-05
Structure title titleKRas G12V, bound to GppNHp and miniprotein 225-11
Keywords keywordsInhibitor, Complex, 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_guinier40.62
Radius of gyration Rg (electron density) rg_electron40.72
Forward intensity I(0) i0175455000.00
Molecular weight molecular_weight102880.0 kDa
Excluded volume excluded_volume126760 ų
Envelope volume envelope_volume172230 ų
Hydration-shell volume shell_volume38584 ų
Envelope diameter envelope_diameter149.5
Shell Rg shell_rg41.50
Envelope Rg envelope_rg40.38
Shape Rg shape_rg40.69
Total Rg total_rg40.86
Total atoms total_atoms7212
Residues n_residues871
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 dmax144.6
Rg (real space) rg_real41.00
Rg uncertainty (real space) rg_real_error1.56
I(0) (real space) i0_real1.7550e+08
I(0) uncertainty (real space) i0_real_error2.7440e+06
Rg (reciprocal space) rg_reciprocal40.62
I(0) (reciprocal space) i0_reciprocal175400000.0000
Solution quality estimate total_estimate0.5628
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary33.4
Skewness Skewness skewness0.550
Kurtosis Kurtosis kurtosis-0.308
Angular range angular_range— – 0.1950 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha20260000.0000
Real-space data points n_real_points40
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.683; Stabil: 1.000; Sysdev: 0.025; Positv: 1.000; Valcen: 0.482; Smooth: 0.707

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

7. Fold Classification (SCOP + CATH) 4 domains

CATH v4.4 (4 domains)

Domain ID domain_id5wplA00
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_id5wplD00
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_id5wplG00
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_id5wplJ00
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)