8xva

Human TOM complex with whole Tom20

Method: ELECTRON MICROSCOPY Dmax: 120.5 Å Quality: GOOD

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

Mitochondrial import receptor subunit TOM6 homolog

OrganismNot specified

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 × 11 PDB declaration: 11-meric(11) Consistent with protein copy count Chain A; UniProt 1–74 Chain F; UniProt 1–74 Not recorded Mitochondrial import receptor subunit TOM40 homolog × 2 (O96008) Mitochondrial import receptor subunit TOM22 homolog × 2 (Q9NS69) Mitochondrial import receptor subunit TOM5 homolog × 2 (Q8N4H5) Mitochondrial import receptor subunit TOM7 homolog × 2 (Q9P0U1) Mitochondrial import receptor subunit TOM20 homolog × 1 (Q15388) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 5.92 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 1
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 TOM40 homolog

OrganismNot specified

UniProt O96008

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 × 11 PDB declaration: 11-meric(11) Consistent with protein copy count Chain B; UniProt 1–361 Chain I; UniProt 1–361 Not recorded Mitochondrial import receptor subunit TOM6 homolog × 2 (Q96B49) Mitochondrial import receptor subunit TOM22 homolog × 2 (Q9NS69) Mitochondrial import receptor subunit TOM5 homolog × 2 (Q8N4H5) Mitochondrial import receptor subunit TOM7 homolog × 2 (Q9P0U1) Mitochondrial import receptor subunit TOM20 homolog × 1 (Q15388) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 5.92 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.

10 other PDB entries and 10 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TOM40_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–361; UniProt 1–361 Author chain I; PDBConstruct 1–361; UniProt 1–361

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 × 11 PDB declaration: 11-meric(11) Consistent with protein copy count Chain C; UniProt 1–142 Chain H; UniProt 1–142 Not recorded Mitochondrial import receptor subunit TOM6 homolog × 2 (Q96B49) Mitochondrial import receptor subunit TOM40 homolog × 2 (O96008) Mitochondrial import receptor subunit TOM5 homolog × 2 (Q8N4H5) Mitochondrial import receptor subunit TOM7 homolog × 2 (Q9P0U1) Mitochondrial import receptor subunit TOM20 homolog × 1 (Q15388) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 5.92 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 3
Chains and sequence ranges Author chain C; PDBConstruct 1–142; UniProt 1–142 Author chain H; PDBConstruct 1–142; UniProt 1–142

Mitochondrial import receptor subunit TOM5 homolog

OrganismNot specified

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 × 11 PDB declaration: 11-meric(11) Consistent with protein copy count Chain D; UniProt 1–51 Chain E; UniProt 1–51 Not recorded Mitochondrial import receptor subunit TOM6 homolog × 2 (Q96B49) Mitochondrial import receptor subunit TOM40 homolog × 2 (O96008) Mitochondrial import receptor subunit TOM22 homolog × 2 (Q9NS69) Mitochondrial import receptor subunit TOM7 homolog × 2 (Q9P0U1) Mitochondrial import receptor subunit TOM20 homolog × 1 (Q15388) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 5.92 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 4
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

OrganismNot specified

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 × 11 PDB declaration: 11-meric(11) Consistent with protein copy count Chain G; UniProt 1–55 Chain J; UniProt 1–55 Not recorded Mitochondrial import receptor subunit TOM6 homolog × 2 (Q96B49) Mitochondrial import receptor subunit TOM40 homolog × 2 (O96008) Mitochondrial import receptor subunit TOM22 homolog × 2 (Q9NS69) Mitochondrial import receptor subunit TOM5 homolog × 2 (Q8N4H5) Mitochondrial import receptor subunit TOM20 homolog × 1 (Q15388) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 5.92 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 5
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 TOM20 homolog

OrganismNot specified

UniProt Q15388

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 × 11 PDB declaration: 11-meric(11) Consistent with protein copy count Chain K; UniProt 1–145 Not recorded Mitochondrial import receptor subunit TOM6 homolog × 2 (Q96B49) Mitochondrial import receptor subunit TOM40 homolog × 2 (O96008) Mitochondrial import receptor subunit TOM22 homolog × 2 (Q9NS69) Mitochondrial import receptor subunit TOM5 homolog × 2 (Q8N4H5) Mitochondrial import receptor subunit TOM7 homolog × 2 (Q9P0U1) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 5.92 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.

10 other PDB entries and 13 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TOM20_HUMAN
Isoform
PDB entities 6
Chains and sequence ranges Author chain K; PDBConstruct 1–145; UniProt 1–145

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 8xva

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id8xva
Deposition date deposition_date2024-01-14
Structure title titleHuman TOM complex with whole Tom20
Keywords keywordsmitochondria, transport, membrane protein complex, PROTEIN TRANSPORT; PROTEIN TRANSPORT
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier37.69
Radius of gyration Rg (electron density) rg_electron37.44
Forward intensity I(0) i0139125000.00
Molecular weight molecular_weight75843.0 kDa
Excluded volume excluded_volume87148 ų
Envelope volume envelope_volume186100 ų
Hydration-shell volume shell_volume44148 ų
Envelope diameter envelope_diameter127.3
Shell Rg shell_rg40.87
Envelope Rg envelope_rg35.60
Shape Rg shape_rg37.43
Total Rg total_rg37.75
Total atoms total_atoms5415
Residues n_residues1100
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 dmax120.5
Rg (real space) rg_real37.55
Rg uncertainty (real space) rg_real_error0.76
I(0) (real space) i0_real1.3910e+08
I(0) uncertainty (real space) i0_real_error2.0880e+06
Rg (reciprocal space) rg_reciprocal37.64
I(0) (reciprocal space) i0_reciprocal139100000.0000
Solution quality estimate total_estimate0.8988
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary43.0
Skewness Skewness skewness0.188
Kurtosis Kurtosis kurtosis-0.472
Angular range angular_range— – 0.2100 −1
Current regularization parameter α current_alpha0.0003
Highest regularization parameter α highest_alpha13520000.0000
Real-space data points n_real_points43
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.911; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.986; Smooth: 0.961

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

8. Citations (1)

9. Files and Curves (10)