7vby

Tom core complex with Tom20 and Tom22 subunits.

Method: ELECTRON MICROSCOPY Dmax: 118.2 Å Quality: GOOD

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

Mitochondrial import receptor subunit TOM6 homolog

Homo sapiens

UniProt Q96B49

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 × 10 PDB declaration: decameric(10) Consistent with protein copy count Chain A; UniProt 1–74 Chain F; UniProt 1–74 Not recorded Translocase of the Outer Membrane × 2 Mitochondrial import receptor subunit TOM5 homolog × 2 (Q8N4H5) Mitochondrial import receptor subunit TOM7 homolog × 2 (Q9P0U1) Mitochondrial import receptor subunit TOM22 homolog × 2 (Q9NS69) PC1 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE × 11 UND UNDECANE × 12 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.54 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.

11 other PDB entries and 11 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TOM6_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain A; PDBConstruct 1–74; UniProt 1–74 Author chain F; PDBConstruct 1–74; UniProt 1–74

Mitochondrial import receptor subunit TOM5 homolog

Homo sapiens

UniProt Q8N4H5

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 × 10 PDB declaration: decameric(10) Consistent with protein copy count Chain D; UniProt 1–51 Chain E; UniProt 1–51 Not recorded Translocase of the Outer Membrane × 2 Mitochondrial import receptor subunit TOM6 homolog × 2 (Q96B49) Mitochondrial import receptor subunit TOM7 homolog × 2 (Q9P0U1) Mitochondrial import receptor subunit TOM22 homolog × 2 (Q9NS69) PC1 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE × 11 UND UNDECANE × 12 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.54 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.

11 other PDB entries and 11 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TOM5_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain D; PDBConstruct 1–51; UniProt 1–51 Author chain E; PDBConstruct 1–51; UniProt 1–51

Mitochondrial import receptor subunit TOM7 homolog

Homo sapiens

UniProt Q9P0U1

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 × 10 PDB declaration: decameric(10) Consistent with protein copy count Chain G; UniProt 1–55 Chain J; UniProt 1–55 Not recorded Translocase of the Outer Membrane × 2 Mitochondrial import receptor subunit TOM6 homolog × 2 (Q96B49) Mitochondrial import receptor subunit TOM5 homolog × 2 (Q8N4H5) Mitochondrial import receptor subunit TOM22 homolog × 2 (Q9NS69) PC1 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE × 11 UND UNDECANE × 12 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.54 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.

11 other PDB entries and 11 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TOM7_HUMAN
Isoform
PDB entities 4
Chains and sequence ranges Author chain G; PDBConstruct 1–55; UniProt 1–55 Author chain J; PDBConstruct 1–55; UniProt 1–55

Mitochondrial import receptor subunit TOM22 homolog

Homo sapiens

UniProt Q9NS69

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 × 10 PDB declaration: decameric(10) Consistent with protein copy count Chain C; UniProt 1–142 Chain H; UniProt 1–142 Not recorded Translocase of the Outer Membrane × 2 Mitochondrial import receptor subunit TOM6 homolog × 2 (Q96B49) Mitochondrial import receptor subunit TOM5 homolog × 2 (Q8N4H5) Mitochondrial import receptor subunit TOM7 homolog × 2 (Q9P0U1) PC1 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE × 11 UND UNDECANE × 12 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.54 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.

11 other PDB entries and 11 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TOM22_HUMAN
Isoform
PDB entities 5
Chains and sequence ranges Author chain C; PDBConstruct 1–142; UniProt 1–142 Author chain H; PDBConstruct 1–142; UniProt 1–142

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 7vby

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id7vby
Deposition date deposition_date2021-09-01
Structure title titleTom core complex with Tom20 and Tom22 subunits.
Keywords keywordsTom complex, Tom20, Cryo-EM, TRANSLOCASE; TRANSLOCASE
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier36.65
Radius of gyration Rg (electron density) rg_electron36.37
Forward intensity I(0) i0168624000.00
Molecular weight molecular_weight116660.0 kDa
Excluded volume excluded_volume151830 ų
Envelope volume envelope_volume221600 ų
Hydration-shell volume shell_volume50923 ų
Envelope diameter envelope_diameter130.0
Shell Rg shell_rg42.37
Envelope Rg envelope_rg36.05
Shape Rg shape_rg36.34
Total Rg total_rg37.01
Total atoms total_atoms9463
Residues n_residues951
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 dmax118.2
Rg (real space) rg_real36.59
Rg uncertainty (real space) rg_real_error0.86
I(0) (real space) i0_real1.6860e+08
I(0) uncertainty (real space) i0_real_error2.6160e+06
Rg (reciprocal space) rg_reciprocal36.63
I(0) (reciprocal space) i0_reciprocal168600000.0000
Solution quality estimate total_estimate0.8903
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary41.2
Skewness Skewness skewness0.281
Kurtosis Kurtosis kurtosis-0.407
Angular range angular_range— – 0.2150 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha14640000.0000
Real-space data points n_real_points44
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.883; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.920

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

8. Citations (1)

9. Files and Curves (10)