7d0e

Crystal structure of FIP200 Claw/p-CCPG1 FIR2

Method: X-RAY DIFFRACTION Dmax: 57.3 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 heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 1490–1594 Not recorded Cell cycle progression protein 1 FIR2 × 2 (Q9ULG6) GO9 3-(2-hydroxyethyloxy)-2-[2-(2-hydroxyethyloxy)ethoxymethyl]-2-(2-hydroxyethyloxymethyl)propan-1-ol × 2 PEG DI(HYDROXYETHYL)ETHER × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;289 K;KCl, Pentaerythritol ethoxylate (15/4 EO/OH), MES Resolution 1.40 Å R-free 0.207

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 1–105; UniProt 1490–1594

Cell cycle progression protein 1 FIR2

Homo sapiens

UniProt Q9ULG6

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain B; UniProt 101–113 Non-standard monomer:Yes (specific site not provided by mmCIF) RB1-inducible coiled-coil protein 1 × 2 (Q8TDY2) GO9 3-(2-hydroxyethyloxy)-2-[2-(2-hydroxyethyloxy)ethoxymethyl]-2-(2-hydroxyethyloxymethyl)propan-1-ol × 2 PEG DI(HYDROXYETHYL)ETHER × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;289 K;KCl, Pentaerythritol ethoxylate (15/4 EO/OH), MES Resolution 1.40 Å R-free 0.207

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 CCPG1_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–13; UniProt 101–113

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 7d0e

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7d0e
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7d0e
Deposition date deposition_date2020-09-09
Structure title titleCrystal structure of FIP200 Claw/p-CCPG1 FIR2
Keywords keywordsautophagy, FIP200, CCPG1, SIGNALING PROTEIN, SIGNALING PROTEIN-PROTEIN BINDING complex; SIGNALING PROTEIN/PROTEIN BINDING
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier15.49
Radius of gyration Rg (electron density) rg_electron14.05
Forward intensity I(0) i03175940.00
Molecular weight molecular_weight12891.0 kDa
Excluded volume excluded_volume16390 ų
Envelope volume envelope_volume19035 ų
Hydration-shell volume shell_volume11745 ų
Envelope diameter envelope_diameter54.2
Shell Rg shell_rg19.54
Envelope Rg envelope_rg14.53
Shape Rg shape_rg13.98
Total Rg total_rg15.48
Total atoms total_atoms908
Residues n_residues106
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 dmax57.3
Rg (real space) rg_real15.46
Rg uncertainty (real space) rg_real_error0.51
I(0) (real space) i0_real3.1760e+06
I(0) uncertainty (real space) i0_real_error4.1470e+04
Rg (reciprocal space) rg_reciprocal15.47
I(0) (reciprocal space) i0_reciprocal3176000.0000
Solution quality estimate total_estimate0.8124
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary20.3
Skewness Skewness skewness0.355
Kurtosis Kurtosis kurtosis0.056
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1124000.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.551; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.908; Smooth: 0.997

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)