1d7m

COILED-COIL DIMERIZATION DOMAIN FROM CORTEXILLIN I

Method: X-RAY DIFFRACTION Dmax: 147.3 Å Quality: REASONABLE

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

CORTEXILLIN I

Dictyostelium discoideum

UniProt O15813

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 243–343 Chain B; UniProt 243–343 Fragment:COILED-COIL DIMERIZATION DOMAIN No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;297 K;1.5 M AMMONIUM SULFATE 100 MM TRIS (PH 6.5) 2.5 % PEG 400 1.0 % DIOXANE, VAPOR DIFFUSION, HANGING DROP, temperature 297K Resolution 2.70 Å R-free 0.249
2 Protein homooligomer Homooligomer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 243–343 Chain B; UniProt 243–343 Fragment:COILED-COIL DIMERIZATION DOMAIN No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;297 K;1.5 M AMMONIUM SULFATE 100 MM TRIS (PH 6.5) 2.5 % PEG 400 1.0 % DIOXANE, VAPOR DIFFUSION, HANGING DROP, temperature 297K Resolution 2.70 Å R-free 0.249

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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name O15813_DICDI
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–101; UniProt 243–343 Author chain B; PDBConstruct 1–101; UniProt 243–343

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 1d7m

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1d7m
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1d7m
Deposition date deposition_date1999-10-19
Structure title titleCOILED-COIL DIMERIZATION DOMAIN FROM CORTEXILLIN I
Keywords keywordsCOILED-COIL, COILED-COIL TRIGGER SITE, ALPHA HELIX, DIMERIZATION, CONTRACTILE PROTEIN; CONTRACTILE PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier40.74
Radius of gyration Rg (electron density) rg_electron42.83
Forward intensity I(0) i09310000.00
Molecular weight molecular_weight23197.0 kDa
Excluded volume excluded_volume28994 ų
Envelope volume envelope_volume41829 ų
Hydration-shell volume shell_volume11940 ų
Envelope diameter envelope_diameter154.1
Shell Rg shell_rg30.74
Envelope Rg envelope_rg43.95
Shape Rg shape_rg42.78
Total Rg total_rg41.93
Total atoms total_atoms1622
Residues n_residues202
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 dmax147.3
Rg (real space) rg_real41.87
Rg uncertainty (real space) rg_real_error2.31
I(0) (real space) i0_real9.3100e+06
I(0) uncertainty (real space) i0_real_error2.2150e+05
Rg (reciprocal space) rg_reciprocal40.74
I(0) (reciprocal space) i0_reciprocal9299000.0000
Solution quality estimate total_estimate0.5702
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary143.6
Skewness Skewness skewness0.691
Kurtosis Kurtosis kurtosis-0.338
Angular range angular_range— – 0.1950 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha308000.0000
Real-space data points n_real_points40
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.028; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.007; Smooth: 0.318

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1d7ma_
Class classh — Coiled coil proteins
Fold Fold foldh.1 — Parallel coiled-coil
Superfamily Superfamily superfamilyh.1.10 — Coiled-coil dimerization domain from cortexillin I
Family Family familyh.1.10.1 — Coiled-coil dimerization domain from cortexillin I
Domain ID domain_idd1d7mb_
Class classh — Coiled coil proteins
Fold Fold foldh.1 — Parallel coiled-coil
Superfamily Superfamily superfamilyh.1.10 — Coiled-coil dimerization domain from cortexillin I
Family Family familyh.1.10.1 — Coiled-coil dimerization domain from cortexillin I

CATH v4.4 (2 domains)

Domain ID domain_id1d7mA00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily340
Domain ID domain_id1d7mB00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily340

8. Citations (2)

9. Files and Curves (10)