6fnz

Crystal Structure of domain-swapped C-terminal domain of human doublecortin

Method: X-RAY DIFFRACTION Dmax: 80.7 Å Quality: REASONABLE

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

Neuronal migration protein doublecortin

Homo sapiens

UniProt O43602

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 174–254 Chain C; UniProt 174–254 Fragment:C-terminal ubiquitin-like domain, UNP residues 174-254 possible peptide × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.3;293 K;20 mg/mL protein and 3x cmc CHAPS in 20mM CAPS/NaOH pH10.5, 100mM NaCl, 5mM TCEP mixed 60-70% with 40-30% reservoir consisting of 0.1M HEPES/NaOH pH7.0, 10% PEG 5000 MME, 5% Tacsimate Resolution 2.23 Å R-free 0.231
2 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain B; UniProt 174–254 Chain D; UniProt 174–254 Fragment:C-terminal ubiquitin-like domain, UNP residues 174-254 possible peptide × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.3;293 K;20 mg/mL protein and 3x cmc CHAPS in 20mM CAPS/NaOH pH10.5, 100mM NaCl, 5mM TCEP mixed 60-70% with 40-30% reservoir consisting of 0.1M HEPES/NaOH pH7.0, 10% PEG 5000 MME, 5% Tacsimate Resolution 2.23 Å R-free 0.231

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.

13 other PDB entries and 22 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name DCX_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–81; UniProt 174–254 Author chain B; PDBConstruct 1–81; UniProt 174–254 Author chain C; PDBConstruct 1–81; UniProt 174–254 Author chain D; PDBConstruct 1–81; UniProt 174–254

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 6fnz

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6fnz
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6fnz
Deposition date deposition_date2018-02-05
Structure title titleCrystal Structure of domain-swapped C-terminal domain of human doublecortin
Keywords keywordsDCX DOMAIN, UBIQUITIN-LIKE FOLD, MICROTUBULE ASSOCIATED, SIGNALING PROTEIN, DOMAIN SWAP, ANALYTICAL ULTRACENTRIFUGATION; SIGNALING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier25.62
Radius of gyration Rg (electron density) rg_electron24.37
Forward intensity I(0) i021555100.00
Molecular weight molecular_weight36923.0 kDa
Excluded volume excluded_volume47106 ų
Envelope volume envelope_volume64626 ų
Hydration-shell volume shell_volume22243 ų
Envelope diameter envelope_diameter84.1
Shell Rg shell_rg31.21
Envelope Rg envelope_rg24.05
Shape Rg shape_rg24.37
Total Rg total_rg25.30
Total atoms total_atoms2598
Residues n_residues333
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 dmax80.7
Rg (real space) rg_real25.55
Rg uncertainty (real space) rg_real_error0.52
I(0) (real space) i0_real2.1560e+07
I(0) uncertainty (real space) i0_real_error2.5300e+05
Rg (reciprocal space) rg_reciprocal25.57
I(0) (reciprocal space) i0_reciprocal21560000.0000
Solution quality estimate total_estimate0.7444
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary36.4
Skewness Skewness skewness0.141
Kurtosis Kurtosis kurtosis-0.618
Angular range angular_range— – 0.3100 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha11730000.0000
Real-space data points n_real_points63
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.926; Stabil: 0.999; Sysdev: 0.315; Positv: 1.000; Valcen: 0.991; Smooth: 0.963

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)