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6sh3

Structure of the ADP state of the heptameric Bcs1 AAA-ATPase

Method: ELECTRON MICROSCOPY Dmax: 152.6 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

Mitochondrial chaperone BCS1

OrganismNot specified

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 homooligomer Homooligomer Protein × 7 PDB declaration: heptameric（7） 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 ADP ADENOSINE-5'-DIPHOSPHATE × 7 ELECTRON MICROSCOPY cryo-EM buffer：pH 8 cryo-EM vitrification conditions：Cryogen ETHANE Resolution 3.40 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.

Other PDB Difference from Current Entry 6SH3 Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
6SH4 Structure of the Apo1 state of the heptameric Bcs1 AAA-ATPase. Deposited 2019-08-05 Different ligand/ion Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 7 PDB declaration: heptameric
Chain A 1–456（456 aa）
Chain B 1–456（456 aa）
Chain C 1–456（456 aa）
Chain D 1–456（456 aa）
Chain E 1–456（456 aa）
Chain F 1–456（456 aa）
Chain G 1–456（456 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 4.40 Å
6SH5 Structure of the Apo2 state of the heptameric Bcs1 AAA-ATPase Deposited 2019-08-05 Different ligand/ion Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 7 PDB declaration: heptameric
Chain A 1–456（456 aa）
Chain B 1–456（456 aa）
Chain C 1–456（456 aa）
Chain D 1–456（456 aa）
Chain E 1–456（456 aa）
Chain F 1–456（456 aa）
Chain G 1–456（456 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 4.60 Å
9GS2 Structure of the Rieske bound Apo1 state of the heptameric Bcs1 AAA-ATPase Deposited 2024-09-13 Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric
Chain A 1–456（456 aa）
Chain B 1–456（456 aa）
Chain C 1–456（456 aa）
Chain D 1–456（456 aa）
Chain E 1–456（456 aa）
Chain F 1–456（456 aa）
Chain G 1–456（456 aa）
Not recorded FES FE2/S2 (INORGANIC) CLUSTER × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.46 Å
9GSN Structure of the ATPgS-S1 state of the heptameric Bcs1 AAA-ATPase Deposited 2024-09-16 Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 7 PDB declaration: heptameric
Chain A 1–456（456 aa）
Chain B 1–456（456 aa）
Chain C 1–456（456 aa）
Chain D 1–456（456 aa）
Chain E 1–456（456 aa）
Chain F 1–456（456 aa）
Chain G 1–456（456 aa）
Not recorded AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 7 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.58 Å
9GU9 Structure of the ATPgS-S2 state of the heptameric Bcs1 AAA-ATPase Deposited 2024-09-19 Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 7 PDB declaration: heptameric
Chain A 1–456（456 aa）
Chain B 1–456（456 aa）
Chain C 1–456（456 aa）
Chain D 1–456（456 aa）
Chain E 1–456（456 aa）
Chain F 1–456（456 aa）
Chain G 1–456（456 aa）
Not recorded AGS PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER × 7 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.74 Å

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 1–456； UniProt 1–456 Author chain B； PDBConstruct 1–456； UniProt 1–456 Author chain C； PDBConstruct 1–456； UniProt 1–456 Author chain D； PDBConstruct 1–456； UniProt 1–456 Author chain E； PDBConstruct 1–456； UniProt 1–456 Author chain F； PDBConstruct 1–456； UniProt 1–456 Author chain G； PDBConstruct 1–456； UniProt 1–456

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 6sh3

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6sh3
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6sh3
Deposition date deposition_date2019-08-05
Structure title titleStructure of the ADP state of the heptameric Bcs1 AAA-ATPase
Keywords keywordstranslocation, Rieske, mitochondira, inner mitochondiral membrane, TRANSLOCASE; TRANSLOCASE
Experimental Method methodELECTRON MICROSCOPY
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier49.98 Å
Radius of gyration Rg (electron density) rg_electron49.64 Å
Forward intensity I(0) i01257370000.00
Molecular weight molecular_weight298960.0 kDa
Excluded volume excluded_volume376190 ų
Envelope volume envelope_volume601450 ų
Hydration-shell volume shell_volume99920 ų
Envelope diameter envelope_diameter148.9 Å
Shell Rg shell_rg55.86 Å
Envelope Rg envelope_rg47.11 Å
Shape Rg shape_rg49.62 Å
Total Rg total_rg49.95 Å
Total atoms total_atoms21021
Residues n_residues2632
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−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
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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax152.6 Å
Rg (real space) rg_real49.51 Å
Rg uncertainty (real space) rg_real_error1.12 Å
I(0) (real space) i0_real1.2570e+09
I(0) uncertainty (real space) i0_real_error2.5620e+07
Rg (reciprocal space) rg_reciprocal49.98 Å
I(0) (reciprocal space) i0_reciprocal1258000000.0000
Solution quality estimate total_estimate0.8935
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary62.0 Å
Skewness Skewness skewness-0.022
Kurtosis Kurtosis kurtosis-0.600
Angular range angular_range— – 0.1600 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha64230000.0000
Real-space data points n_real_points33
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.916; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.959; Smooth: 0.904
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (2)

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8. Citations (1)

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9. Files and Curves (10)