6dce

X-ray structure of FIP200 claw domain

Method: X-RAY DIFFRACTION Dmax: 47.8 Å Quality: GOOD

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

RB1-inducible coiled-coil protein 1

Homo sapiens

UniProt Q8TDY2

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 1494–1594 Non-standard monomer:Yes (specific site not provided by mmCIF) SO4 SULFATE ION × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;292 K;0.1 M HEPES pH 7.4, 2 M Ammonium sulfate Resolution 1.56 Å R-free 0.241

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.

17 other PDB entries and 26 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RBCC1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–101; UniProt 1494–1594

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 6dce

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id6dce
Deposition date deposition_date2018-05-05
Structure title titleX-ray structure of FIP200 claw domain
Keywords keywordsautophagy, FIP200, STRUCTURAL PROTEIN; STRUCTURAL PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier14.15
Radius of gyration Rg (electron density) rg_electron12.91
Forward intensity I(0) i02500420.00
Molecular weight molecular_weight11048.0 kDa
Excluded volume excluded_volume13905 ų
Envelope volume envelope_volume15776 ų
Hydration-shell volume shell_volume10546 ų
Envelope diameter envelope_diameter46.5
Shell Rg shell_rg18.44
Envelope Rg envelope_rg13.29
Shape Rg shape_rg12.85
Total Rg total_rg14.37
Total atoms total_atoms773
Residues n_residues91
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 dmax47.8
Rg (real space) rg_real14.07
Rg uncertainty (real space) rg_real_error0.28
I(0) (real space) i0_real2.5000e+06
I(0) uncertainty (real space) i0_real_error2.6060e+04
Rg (reciprocal space) rg_reciprocal14.07
I(0) (reciprocal space) i0_reciprocal2500000.0000
Solution quality estimate total_estimate0.7867
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary47.2
Skewness Skewness skewness0.192
Kurtosis Kurtosis kurtosis-0.225
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha639500.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.741; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)