1far

RAF-1 CYSTEINE RICH DOMAIN, NMR, MINIMIZED AVERAGE STRUCTURE

Method: SOLUTION NMR Dmax: 41.1 Å Quality: GOOD

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

RAF-1

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 136–187 Fragment:CYSTEINE-RICH DOMAIN ZN ZINC ION × 2 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 1–52; UniProt 136–187

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 1far

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1far
Deposition date deposition_date1996-09-05
Structure title titleRAF-1 CYSTEINE RICH DOMAIN, NMR, MINIMIZED AVERAGE STRUCTURE
Keywords keywords;TRANSFERASE, SERINE/THREONINE-PROTEIN KINASE, PROTO-ONCOGENE, ZINC, ATP-BINDING, PHORBOL-ESTER BINDING, 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_guinier11.97
Radius of gyration Rg (electron density) rg_electron11.17
Forward intensity I(0) i0985242.00
Molecular weight molecular_weight6268.0 kDa
Excluded volume excluded_volume7755 ų
Envelope volume envelope_volume9155 ų
Hydration-shell volume shell_volume7401 ų
Envelope diameter envelope_diameter38.7
Shell Rg shell_rg16.16
Envelope Rg envelope_rg11.71
Shape Rg shape_rg11.20
Total Rg total_rg12.52
Total atoms total_atoms846
Residues n_residues52
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 dmax41.1
Rg (real space) rg_real11.95
Rg uncertainty (real space) rg_real_error0.26
I(0) (real space) i0_real9.8520e+05
I(0) uncertainty (real space) i0_real_error9.5140e+03
Rg (reciprocal space) rg_reciprocal11.95
I(0) (reciprocal space) i0_reciprocal985200.0000
Solution quality estimate total_estimate0.8700
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary14.6
Skewness Skewness skewness0.306
Kurtosis Kurtosis kurtosis-0.143
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha123000.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.781; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.979; Smooth: 0.983

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1fara_
Class classg — Small proteins
Fold Fold foldg.49 — Cysteine-rich domain
Superfamily Superfamily superfamilyg.49.1 — Cysteine-rich domain
Family Family familyg.49.1.1 — Protein kinase cysteine-rich domain (cys2, phorbol-binding domain)

CATH v4.4 (1 domains)

Domain ID domain_id1farA00
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology60 — Wheat Germ Agglutinin (Isolectin 2); domain 1
Homologous superfamily homologous superfamily20

8. Citations (1)

9. Files and Curves (10)