1rfa

NMR SOLUTION STRUCTURE OF THE RAS-BINDING DOMAIN OF C-RAF-1

Method: SOLUTION NMR Dmax: 37.5 Å Quality: GOOD

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

RAF1

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 55–132 Fragment:RAS BINDING DOMAIN, RESIDUES 55 - 132 WITH AN ADDITIONAL ALA AT THE N-TERMINUS No other associated polymer SOLUTION NMR mmCIF provides none of the parsed experimental conditions 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 2–79; UniProt 55–132

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 1rfa

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1rfa
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1rfa
Deposition date deposition_date1995-04-26
Structure title titleNMR SOLUTION STRUCTURE OF THE RAS-BINDING DOMAIN OF C-RAF-1
Keywords keywordsSERINE/THREONINE-PROTEIN KINASE, SIGNAL TRANSDUCTION PROTEIN, SERINE-THREONINE-PROTEIN KINASE complex; SERINE/THREONINE-PROTEIN KINASE
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier11.79
Radius of gyration Rg (electron density) rg_electron11.53
Forward intensity I(0) i01016150000.00
Molecular weight molecular_weight266770.0 kDa
Excluded volume excluded_volume333060 ų
Envelope volume envelope_volume17569 ų
Hydration-shell volume shell_volume11379 ų
Envelope diameter envelope_diameter44.6
Shell Rg shell_rg18.96
Envelope Rg envelope_rg13.51
Shape Rg shape_rg11.50
Total Rg total_rg11.74
Total atoms total_atoms37947
Residues n_residues2340
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 dmax37.5
Rg (real space) rg_real11.69
Rg uncertainty (real space) rg_real_error0.26
I(0) (real space) i0_real1.0160e+09
I(0) uncertainty (real space) i0_real_error1.0930e+07
Rg (reciprocal space) rg_reciprocal11.69
I(0) (reciprocal space) i0_reciprocal1016000000.0000
Solution quality estimate total_estimate0.8723
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary16.2
Skewness Skewness skewness-0.061
Kurtosis Kurtosis kurtosis-0.371
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha124500.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.794; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.984; Smooth: 0.972

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1rfaa_
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 (1 domains)

Domain ID domain_id1rfaA00
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 (3)

9. Files and Curves (10)