1mjd

Structure of N-terminal domain of human doublecortin

Method: SOLUTION NMR Dmax: 43.9 Å Quality: REASONABLE

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

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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 87–192 Fragment:N-terminal domain, Residues (45-150) No other associated polymer SOLUTION NMR NMR measurement conditions:pH 6;298 K;Pressure ambient NMR sample composition:1mM doublecortin 45-150 U-15N, 13C; 50mM phosphate buffer; 5mMM DTT | 90% H2O, 10% H2O 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.

13 other PDB entries and 23 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 8–113; UniProt 87–192

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 1mjd

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1mjd
Deposition date deposition_date2002-08-27
Structure title titleStructure of N-terminal domain of human doublecortin
Keywords keywordsDCX domain, ubiquitin-like fold, microtubule associated protein, SIGNALING PROTEIN; SIGNALING PROTEIN
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier15.84
Radius of gyration Rg (electron density) rg_electron15.46
Forward intensity I(0) i0966901000.00
Molecular weight molecular_weight259130.0 kDa
Excluded volume excluded_volume322550 ų
Envelope volume envelope_volume57675 ų
Hydration-shell volume shell_volume21624 ų
Envelope diameter envelope_diameter76.0
Shell Rg shell_rg29.63
Envelope Rg envelope_rg24.41
Shape Rg shape_rg15.42
Total Rg total_rg15.99
Total atoms total_atoms36040
Residues n_residues2260
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 dmax43.9
Rg (real space) rg_real14.79
Rg uncertainty (real space) rg_real_error0.07
I(0) (real space) i0_real9.2320e+08
I(0) uncertainty (real space) i0_real_error7.6710e+06
Rg (reciprocal space) rg_reciprocal16.00
I(0) (reciprocal space) i0_reciprocal966900000.0000
Solution quality estimate total_estimate0.6758
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary17.8
Skewness Skewness skewness0.382
Kurtosis Kurtosis kurtosis-0.098
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha2.6470
Highest regularization parameter α highest_alpha583000.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.005; Oscil: 0.939; Stabil: 0.992; Sysdev: 0.000; Positv: 1.000; Valcen: 0.998; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1mjda1
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.15 — beta-Grasp (ubiquitin-like)
Superfamily Superfamily superfamilyd.15.11 — Doublecortin (DC)
Family Family familyd.15.11.1 — Doublecortin (DC)
Domain ID domain_idd1mjda2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags

CATH v4.4 (1 domains)

Domain ID domain_id1mjdA00
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology20 — Ubiquitin-like (UB roll)
Homologous superfamily homologous superfamily230 — Doublecortin domain

8. Citations (2)

9. Files and Curves (10)