8scx

Cryo-EM structure of the core TIM23 complex from S. cerevisiae

Method: ELECTRON MICROSCOPY Dmax: 106.3 Å Quality: GOOD

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

Mitochondrial import inner membrane translocase subunit TIM17

Saccharomyces cerevisiae

UniProt A0A6A5PVU8

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain A; UniProt 1–158 Not recorded Mitochondrial import inner membrane translocase subunit TIM23 × 1 (A0A6A5Q5E3) Mitochondrial import inner membrane translocase subunit TIM44 × 1 (A0A6A5Q2Y5) Antibody Fab fragment light chain × 1 Antibody Fab fragment heavy chain × 1 CDL CARDIOLIPIN × 1 PTY PHOSPHATIDYLETHANOLAMINE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.70 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 A0A6A5PVU8_YEASX
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–158; UniProt 1–158

Mitochondrial import inner membrane translocase subunit TIM23

Saccharomyces cerevisiae

UniProt A0A6A5Q5E3

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain B; UniProt 1–222 Not recorded Mitochondrial import inner membrane translocase subunit TIM17 × 1 (A0A6A5PVU8) Mitochondrial import inner membrane translocase subunit TIM44 × 1 (A0A6A5Q2Y5) Antibody Fab fragment light chain × 1 Antibody Fab fragment heavy chain × 1 CDL CARDIOLIPIN × 1 PTY PHOSPHATIDYLETHANOLAMINE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.70 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.

2 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A6A5Q5E3_YEASX
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–222; UniProt 1–222

Mitochondrial import inner membrane translocase subunit TIM44

Saccharomyces cerevisiae

UniProt A0A6A5Q2Y5

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain C; UniProt 1–431 Not recorded Mitochondrial import inner membrane translocase subunit TIM17 × 1 (A0A6A5PVU8) Mitochondrial import inner membrane translocase subunit TIM23 × 1 (A0A6A5Q5E3) Antibody Fab fragment light chain × 1 Antibody Fab fragment heavy chain × 1 CDL CARDIOLIPIN × 1 PTY PHOSPHATIDYLETHANOLAMINE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.70 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 A0A6A5Q2Y5_YEASX
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–431; UniProt 1–431

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 8scx

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id8scx
Deposition date deposition_date2023-04-05
Structure title titleCryo-EM structure of the core TIM23 complex from S. cerevisiae
Keywords keywordsTRANSLOCASE; TRANSLOCASE
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier32.94
Radius of gyration Rg (electron density) rg_electron32.48
Forward intensity I(0) i0105206000.00
Molecular weight molecular_weight81732.0 kDa
Excluded volume excluded_volume102410 ų
Envelope volume envelope_volume135780 ų
Hydration-shell volume shell_volume35967 ų
Envelope diameter envelope_diameter115.4
Shell Rg shell_rg38.20
Envelope Rg envelope_rg32.35
Shape Rg shape_rg32.46
Total Rg total_rg33.04
Total atoms total_atoms5753
Residues n_residues760
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 dmax106.3
Rg (real space) rg_real33.00
Rg uncertainty (real space) rg_real_error0.75
I(0) (real space) i0_real1.0520e+08
I(0) uncertainty (real space) i0_real_error1.7030e+06
Rg (reciprocal space) rg_reciprocal32.98
I(0) (reciprocal space) i0_reciprocal105200000.0000
Solution quality estimate total_estimate0.8992
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary35.4
Skewness Skewness skewness0.314
Kurtosis Kurtosis kurtosis-0.546
Angular range angular_range— – 0.2400 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha10910000.0000
Real-space data points n_real_points49
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.938; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.965; Smooth: 0.908

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

8. Citations (1)

9. Files and Curves (10)