6ntd

Crystal Structure of G12V HRas-GppNHp bound in complex with the engineered RBD variant 12 of CRAF Kinase protein

Method: X-RAY DIFFRACTION Dmax: 62.0 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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 1–166 Mutation:G12V RAF proto-oncogene serine/threonine-protein kinase × 1 (P04049) MG MAGNESIUM ION × 1 GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 5.6;293.15 K;30% PEG4000, 200mM NH4SO4, 100mM Na Citrate Resolution 3.15 Å R-free 0.287

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 A; PDBConstruct 6–171; UniProt 1–166

RAF proto-oncogene serine/threonine-protein kinase

Homo sapiens

UniProt P04049

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 B; UniProt 55–131 Mutation:F61L, K65H, Q66E, N71K, C81S, V88R, R89H, C95S, C96S GTPase HRas × 1 (P01112) MG MAGNESIUM ION × 1 GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 5.6;293.15 K;30% PEG4000, 200mM NH4SO4, 100mM Na Citrate Resolution 3.15 Å R-free 0.287

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.

74 other PDB entries and 83 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RAF1_HUMAN
Isoform P04049-2
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 5–81; UniProt 55–131

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 6ntd

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id6ntd
Deposition date deposition_date2019-01-28
Structure title titleCrystal Structure of G12V HRas-GppNHp bound in complex with the engineered RBD variant 12 of CRAF Kinase protein
Keywords keywordsaffinity reagent, engineered protein, RAS inhibitor, TRANSFERASE-PROTEIN BINDING complex; TRANSFERASE/PROTEIN BINDING
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier18.66
Radius of gyration Rg (electron density) rg_electron17.65
Forward intensity I(0) i011396300.00
Molecular weight molecular_weight23712.0 kDa
Excluded volume excluded_volume29102 ų
Envelope volume envelope_volume34964 ų
Hydration-shell volume shell_volume16907 ų
Envelope diameter envelope_diameter62.4
Shell Rg shell_rg23.51
Envelope Rg envelope_rg17.98
Shape Rg shape_rg17.67
Total Rg total_rg18.49
Total atoms total_atoms1665
Residues n_residues231
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 dmax62.0
Rg (real space) rg_real18.61
Rg uncertainty (real space) rg_real_error0.35
I(0) (real space) i0_real1.1400e+07
I(0) uncertainty (real space) i0_real_error1.5690e+05
Rg (reciprocal space) rg_reciprocal18.62
I(0) (reciprocal space) i0_reciprocal11400000.0000
Solution quality estimate total_estimate0.8763
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary23.8
Skewness Skewness skewness0.300
Kurtosis Kurtosis kurtosis-0.243
Angular range angular_range— – 0.4250 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha2431000.0000
Real-space data points n_real_points74
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.797; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.998

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 5 domains

SCOP 2.08 (3 domains)

Domain ID domain_idd6ntda1
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.37.1.0 — automated matches
Domain ID domain_idd6ntda2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags
Domain ID domain_idd6ntdb_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.15 — beta-Grasp (ubiquitin-like)
Superfamily Superfamily superfamilyd.15.1 — Ubiquitin-like
Family Family familyd.15.1.5 — Ras-binding domain, RBD

CATH v4.4 (2 domains)

Domain ID domain_id6ntdA00
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_id6ntdB00
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology20 — Ubiquitin-like (UB roll)
Homologous superfamily homologous superfamily90 — Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1

8. Citations (1)

9. Files and Curves (10)