7czg

Crystal structure of FIP200 Claw domain apo form

Method: X-RAY DIFFRACTION Dmax: 85.8 Å Quality: REASONABLE

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 homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 1490–1594 Chain C; UniProt 1490–1594 Not recorded PEG DI(HYDROXYETHYL)ETHER × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;289 K;Sodium citrate tribasic dihydrate pH 5.0, Jeffamine ED-2001 pH 7.0 Resolution 1.80 Å R-free 0.230
2 Protein homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 1490–1594 Chain D; UniProt 1490–1594 Not recorded PEG DI(HYDROXYETHYL)ETHER × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;289 K;Sodium citrate tribasic dihydrate pH 5.0, Jeffamine ED-2001 pH 7.0 Resolution 1.80 Å R-free 0.230

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 25 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 4–108; UniProt 1490–1594 Author chain B; PDBConstruct 4–108; UniProt 1490–1594 Author chain C; PDBConstruct 4–108; UniProt 1490–1594 Author chain D; PDBConstruct 4–108; UniProt 1490–1594

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 7czg

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id7czg
Deposition date deposition_date2020-09-08
Structure title titleCrystal structure of FIP200 Claw domain apo form
Keywords keywordsautophagy, FIP200, SIGNALING PROTEIN; SIGNALING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier24.72
Radius of gyration Rg (electron density) rg_electron23.51
Forward intensity I(0) i031002600.00
Molecular weight molecular_weight45363.0 kDa
Excluded volume excluded_volume57980 ų
Envelope volume envelope_volume74639 ų
Hydration-shell volume shell_volume26191 ų
Envelope diameter envelope_diameter93.5
Shell Rg shell_rg30.54
Envelope Rg envelope_rg23.53
Shape Rg shape_rg23.46
Total Rg total_rg24.59
Total atoms total_atoms3209
Residues n_residues389
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 dmax85.8
Rg (real space) rg_real24.57
Rg uncertainty (real space) rg_real_error0.68
I(0) (real space) i0_real3.1000e+07
I(0) uncertainty (real space) i0_real_error4.8750e+05
Rg (reciprocal space) rg_reciprocal24.61
I(0) (reciprocal space) i0_reciprocal31000000.0000
Solution quality estimate total_estimate0.6029
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary32.7
Skewness Skewness skewness0.135
Kurtosis Kurtosis kurtosis-0.455
Angular range angular_range— – 0.3200 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha7223000.0000
Real-space data points n_real_points64
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.769; Stabil: 0.999; Sysdev: 0.184; Positv: 1.000; Valcen: 0.980; 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)