8jof

solution-structure of Ras Binding Domain (RBD) in C-RAF

Method: SOLUTION NMR Dmax: 41.9 Å Quality: GOOD

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

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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 51–131 Not recorded No other associated polymer SOLUTION NMR NMR measurement conditions:pH 6.8;298 K;Ionic strength (raw mmCIF value) 85;Pressure ambient NMR sample composition:0.3 mM [U-100% 13C; U-100% 15N] Serine/threonine-protein Kinase C-RAF, 25 mM sodium phosphate, 50 mM sodium chloride, 10 mM magnesium dichloride, 90% H2O/10% D2O | 90% H2O/10% D2O Resolution not provided

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
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 6–86; UniProt 51–131

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 8jof

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id8jof
Deposition date deposition_date2023-06-07
最后修订 last_revision2024-06-12
Structure title titlesolution-structure of Ras Binding Domain (RBD) in C-RAF
Keywords keywordsMAPK, SIGNALING PROTEIN; SIGNALING PROTEIN
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier13.10
Radius of gyration Rg (electron density) rg_electron12.73
Forward intensity I(0) i0525525000.00
Molecular weight molecular_weight192090.0 kDa
Excluded volume excluded_volume240490 ų
Envelope volume envelope_volume23065 ų
Hydration-shell volume shell_volume13410 ų
Envelope diameter envelope_diameter45.6
Shell Rg shell_rg20.44
Envelope Rg envelope_rg14.78
Shape Rg shape_rg12.70
Total Rg total_rg13.01
Total atoms total_atoms27440
Residues n_residues1720
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 dmax41.9
Rg (real space) rg_real12.99
Rg uncertainty (real space) rg_real_error0.27
I(0) (real space) i0_real5.2550e+08
I(0) uncertainty (real space) i0_real_error5.8180e+06
Rg (reciprocal space) rg_reciprocal13.00
I(0) (reciprocal space) i0_reciprocal525500000.0000
Solution quality estimate total_estimate0.8815
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary16.4
Skewness Skewness skewness0.014
Kurtosis Kurtosis kurtosis-0.435
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha217400.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.824; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.986; Smooth: 0.996

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

8. Citations (1)

9. Files and Curves (10)