9gs2

Structure of the Rieske bound Apo1 state of the heptameric Bcs1 AAA-ATPase

Method: ELECTRON MICROSCOPY Dmax: 145.3 Å Quality: GOOD

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

Mitochondrial chaperone BCS1

Saccharomyces cerevisiae

UniProt P32839

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 × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain A; UniProt 1–456 Chain B; UniProt 1–456 Chain C; UniProt 1–456 Chain D; UniProt 1–456 Chain E; UniProt 1–456 Chain F; UniProt 1–456 Chain G; UniProt 1–456 Not recorded Cytochrome b-c1 complex subunit Rieske, mitochondrial × 1 (P08067) FES FE2/S2 (INORGANIC) CLUSTER × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.46 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.

5 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name BCS1_YEAST
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 25–480; UniProt 1–456 Author chain B; PDBConstruct 25–480; UniProt 1–456 Author chain C; PDBConstruct 25–480; UniProt 1–456 Author chain D; PDBConstruct 25–480; UniProt 1–456 Author chain E; PDBConstruct 25–480; UniProt 1–456 Author chain F; PDBConstruct 25–480; UniProt 1–456 Author chain G; PDBConstruct 25–480; UniProt 1–456

Cytochrome b-c1 complex subunit Rieske, mitochondrial

Saccharomyces cerevisiae

UniProt P08067

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 × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain H; UniProt 92–215 Not recorded Mitochondrial chaperone BCS1 × 7 (P32839) FES FE2/S2 (INORGANIC) CLUSTER × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.46 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.

15 other PDB entries and 15 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name UCRI_YEAST
Isoform
PDB entities 2
Chains and sequence ranges Author chain H; PDBConstruct 1–124; UniProt 92–215

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 9gs2

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9gs2
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9gs2
Deposition date deposition_date2024-09-13
Structure title titleStructure of the Rieske bound Apo1 state of the heptameric Bcs1 AAA-ATPase
Keywords keywordsHeptameric complex Iron-sulfur cluster substrate, TRANSLOCASE; TRANSLOCASE
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier47.29
Radius of gyration Rg (electron density) rg_electron46.97
Forward intensity I(0) i01432300000.00
Molecular weight molecular_weight317710.0 kDa
Excluded volume excluded_volume399140 ų
Envelope volume envelope_volume579980 ų
Hydration-shell volume shell_volume100190 ų
Envelope diameter envelope_diameter144.2
Shell Rg shell_rg54.24
Envelope Rg envelope_rg45.05
Shape Rg shape_rg46.95
Total Rg total_rg47.31
Total atoms total_atoms22365
Residues n_residues2798
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 dmax145.3
Rg (real space) rg_real46.88
Rg uncertainty (real space) rg_real_error1.07
I(0) (real space) i0_real1.4320e+09
I(0) uncertainty (real space) i0_real_error2.8120e+07
Rg (reciprocal space) rg_reciprocal47.29
I(0) (reciprocal space) i0_reciprocal1433000000.0000
Solution quality estimate total_estimate0.8853
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary61.6
Skewness Skewness skewness0.013
Kurtosis Kurtosis kurtosis-0.507
Angular range angular_range— – 0.1650 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha167700000.0000
Real-space data points n_real_points34
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.888; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.950; Smooth: 0.890

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (2)

9. Files and Curves (10)