8r64

Cryo-EM structure of the FIGNL1 AAA hexamer bound to RAD51

Method: ELECTRON MICROSCOPY Dmax: 130.1 Å Quality: EXCELLENT

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

Fidgetin-like protein 1

Homo sapiens

UniProt Q6PIW4

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 × 7 PDB declaration: heptameric(7) Consistent with protein copy count Chain A; UniProt 284–674 Chain B; UniProt 284–674 Chain C; UniProt 284–674 Chain D; UniProt 284–674 Chain E; UniProt 284–674 Chain F; UniProt 284–674 Mutation:E501Q DNA repair protein RAD51 homolog 1 × 1 (Q06609) MG MAGNESIUM ION × 6 ATP ADENOSINE-5'-TRIPHOSPHATE × 5 ADP ADENOSINE-5'-DIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.20 Å

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.

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name FIGL1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 17–407; UniProt 284–674 Author chain B; PDBConstruct 17–407; UniProt 284–674 Author chain C; PDBConstruct 17–407; UniProt 284–674 Author chain D; PDBConstruct 17–407; UniProt 284–674 Author chain E; PDBConstruct 17–407; UniProt 284–674 Author chain F; PDBConstruct 17–407; UniProt 284–674

DNA repair protein RAD51 homolog 1

Homo sapiens

UniProt Q06609

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 × 7 PDB declaration: heptameric(7) Consistent with protein copy count Chain G; UniProt 1–339 Not recorded Fidgetin-like protein 1 × 6 (Q6PIW4) MG MAGNESIUM ION × 6 ATP ADENOSINE-5'-TRIPHOSPHATE × 5 ADP ADENOSINE-5'-DIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.20 Å

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.

50 other PDB entries and 51 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RAD51_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain G; PDBConstruct 1–339; UniProt 1–339

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 8r64

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8r64
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8r64
Deposition date deposition_date2023-11-20
Structure title titleCryo-EM structure of the FIGNL1 AAA hexamer bound to RAD51
Keywords keywordsAAA, ATPase, DNA repair, HYDROLASE; HYDROLASE
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier40.69
Radius of gyration Rg (electron density) rg_electron40.29
Forward intensity I(0) i0557895000.00
Molecular weight molecular_weight191540.0 kDa
Excluded volume excluded_volume239250 ų
Envelope volume envelope_volume330190 ų
Hydration-shell volume shell_volume65943 ų
Envelope diameter envelope_diameter131.8
Shell Rg shell_rg47.53
Envelope Rg envelope_rg39.98
Shape Rg shape_rg40.30
Total Rg total_rg40.65
Total atoms total_atoms13424
Residues n_residues1765
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 dmax130.1
Rg (real space) rg_real40.57
Rg uncertainty (real space) rg_real_error1.13
I(0) (real space) i0_real5.5790e+08
I(0) uncertainty (real space) i0_real_error1.0740e+07
Rg (reciprocal space) rg_reciprocal40.68
I(0) (reciprocal space) i0_reciprocal558000000.0000
Solution quality estimate total_estimate0.9024
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary50.0
Skewness Skewness skewness0.175
Kurtosis Kurtosis kurtosis-0.608
Angular range angular_range— – 0.1950 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha209100000.0000
Real-space data points n_real_points40
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.934; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.926

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (2)

9. Files and Curves (10)