4dnk

Crystal structure of a tyrosine 3-monooxygenase/tryptophan 5-monooxygenase activation protein, beta polypeptide (YWHAB) from homo sapiens at 2.20 A resolution.

Method: X-RAY DIFFRACTION Dmax: 91.0 Å Quality: EXCELLENT

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

14-3-3 protein beta/alpha

Homo sapiens

UniProt P31946

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 homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 1–246 Chain B; UniProt 1–246 Non-standard monomer:Yes (specific site not provided by mmCIF) PO4 PHOSPHATE ION × 3 EDO 1,2-ETHANEDIOL × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;277 K;20.00% polyethylene glycol 3350, 0.20M magnesium acetate, NANODROP, VAPOR DIFFUSION, SITTING DROP, temperature 277K Resolution 2.20 Å R-free 0.226

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.

16 other PDB entries and 24 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name 1433B_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–247; UniProt 1–246 Author chain B; PDBConstruct 2–247; UniProt 1–246

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 4dnk

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4dnk
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4dnk
Deposition date deposition_date2012-02-08
Structure title titleCrystal structure of a tyrosine 3-monooxygenase/tryptophan 5-monooxygenase activation protein, beta polypeptide (YWHAB) from homo sapiens at 2.20 A resolution.
Keywords keywords;14-3-3 domain, phosphorylation, protein-protein binding, cell signaling, cell regulation, Structural Genomics, Joint Center for Structural Genomics, JCSG, Protein Structure Initiative, PSI-BIOLOGY, SIGNALING PROTEIN, Partnership for T-Cell Biology, TCELL ;; SIGNALING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier28.91
Radius of gyration Rg (electron density) rg_electron28.27
Forward intensity I(0) i053364500.00
Molecular weight molecular_weight54604.0 kDa
Excluded volume excluded_volume67163 ų
Envelope volume envelope_volume90820 ų
Hydration-shell volume shell_volume27377 ų
Envelope diameter envelope_diameter93.0
Shell Rg shell_rg34.92
Envelope Rg envelope_rg27.75
Shape Rg shape_rg28.31
Total Rg total_rg28.83
Total atoms total_atoms3780
Residues n_residues451
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 dmax91.0
Rg (real space) rg_real28.92
Rg uncertainty (real space) rg_real_error0.75
I(0) (real space) i0_real5.3360e+07
I(0) uncertainty (real space) i0_real_error8.1070e+05
Rg (reciprocal space) rg_reciprocal28.92
I(0) (reciprocal space) i0_reciprocal53360000.0000
Solution quality estimate total_estimate0.9069
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary33.1
Skewness Skewness skewness0.247
Kurtosis Kurtosis kurtosis-0.659
Angular range angular_range— – 0.2750 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha4866000.0000
Real-space data points n_real_points56
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.964; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.948; Smooth: 0.946

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_idd4dnka_
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_idd4dnkb_
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_id4dnkA00
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_id4dnkB00
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)