3nkx

Impaired binding of 14-3-3 to Raf1 is linked to Noonan and LEOPARD syndrome

Method: X-RAY DIFFRACTION Dmax: 84.9 Å Quality: REASONABLE

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

14-3-3 protein zeta/delta

Homo sapiens

UniProt P63104

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 1–245 Chain B; UniProt 1–245 Not recorded Peptide of RAF proto-oncogene serine/threonine-protein kinase × 2 (P04049) PPI PROPANOIC ACID × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8;293 K;0.1M (Sodium propionate, sodium cacodylate, BIS-TRIS propane), 27% PEG 1500, 2mM DTT, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 2.40 Å R-free 0.247

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.

73 other PDB entries and 88 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name 1433Z_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–245; UniProt 1–245 Author chain B; PDBConstruct 1–245; UniProt 1–245

Peptide of RAF proto-oncogene serine/threonine-protein kinase

OrganismNot specified

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain P; UniProt 255–264 Chain Q; UniProt 255–264 Fragment:phosphorylated C-Raf peptide, UNP residues 255-264 Non-standard monomer:Yes (specific site not provided by mmCIF) 14-3-3 protein zeta/delta × 2 (P63104) PPI PROPANOIC ACID × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8;293 K;0.1M (Sodium propionate, sodium cacodylate, BIS-TRIS propane), 27% PEG 1500, 2mM DTT, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K Resolution 2.40 Å R-free 0.247

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 2
Chains and sequence ranges Author chain P; PDBConstruct 1–10; UniProt 255–264 Author chain Q; PDBConstruct 1–10; UniProt 255–264

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 3nkx

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3nkx
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3nkx
Deposition date deposition_date2010-06-21
Structure title titleImpaired binding of 14-3-3 to Raf1 is linked to Noonan and LEOPARD syndrome
Keywords keywordsPROTEIN BINDING, SIGNALING PROTEIN; PROTEIN BINDING, SIGNALING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier27.24
Radius of gyration Rg (electron density) rg_electron26.50
Forward intensity I(0) i048889500.00
Molecular weight molecular_weight53245.0 kDa
Excluded volume excluded_volume66156 ų
Envelope volume envelope_volume84726 ų
Hydration-shell volume shell_volume26666 ų
Envelope diameter envelope_diameter85.5
Shell Rg shell_rg33.90
Envelope Rg envelope_rg26.03
Shape Rg shape_rg26.51
Total Rg total_rg27.23
Total atoms total_atoms3735
Residues n_residues472
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 dmax84.9
Rg (real space) rg_real27.21
Rg uncertainty (real space) rg_real_error0.55
I(0) (real space) i0_real4.8890e+07
I(0) uncertainty (real space) i0_real_error6.6660e+05
Rg (reciprocal space) rg_reciprocal27.22
I(0) (reciprocal space) i0_reciprocal48890000.0000
Solution quality estimate total_estimate0.7437
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary29.3
Skewness Skewness skewness0.208
Kurtosis Kurtosis kurtosis-0.690
Angular range angular_range— – 0.2900 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha8773000.0000
Real-space data points n_real_points59
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.967; Stabil: 1.000; Sysdev: 0.267; Positv: 1.000; Valcen: 0.985; Smooth: 0.978

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd3nkxa_
Class classa — All alpha proteins
Fold Fold folda.118 — alpha-alpha superhelix
Superfamily Superfamily superfamilya.118.7 — 14-3-3 protein
Family Family familya.118.7.1 — 14-3-3 protein
Domain ID domain_idd3nkxb_
Class classa — All alpha proteins
Fold Fold folda.118 — alpha-alpha superhelix
Superfamily Superfamily superfamilya.118.7 — 14-3-3 protein
Family Family familya.118.7.1 — 14-3-3 protein

CATH v4.4 (2 domains)

Domain ID domain_id3nkxA00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology190 — Delta-Endotoxin; domain 1
Homologous superfamily homologous superfamily20 — 14-3-3 domain
Domain ID domain_id3nkxB00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology190 — Delta-Endotoxin; domain 1
Homologous superfamily homologous superfamily20 — 14-3-3 domain

8. Citations (1)

9. Files and Curves (10)