Research workbench
Crystal structure of rat TOM20-aldh presequence complex
Analyse Crystal structure of rat TOM20-aldh presequence complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2V1S
- Type
- protein
- Length
- 493 residues
- Chains
- 14
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Mitochondrial import receptor subunit TOM20 homolog; Aldehyde dehydrogenase
- EC
- 1.2.1.3
- UniProt
- Q62760, P11884
- Pockets
- 4 · best druggability 0.74
Structure
x-ray diffraction · 11 distinct chains · 73% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Mitochondrial import receptor subunit TOM20 homolog | protein | 66 | 76% helix, 0% strand | Q62760 |
| C | Mitochondrial import receptor subunit TOM20 homolog | protein | 69 | 78% helix, 0% strand | Q62760 |
| D | Mitochondrial import receptor subunit TOM20 homolog | protein | 67 | 73% helix, 0% strand | Q62760 |
| E | Mitochondrial import receptor subunit TOM20 homolog | protein | 71 | 77% helix, 0% strand | Q62760 |
| F | Mitochondrial import receptor subunit TOM20 homolog | protein | 64 | 80% helix, 0% strand | Q62760 |
| G | Mitochondrial import receptor subunit TOM20 homolog | protein | 14 | 64% helix, 0% strand | Q62760 |
| H | Aldehyde dehydrogenase (EC 1.2.1.3) | protein | 12 | 58% helix, 0% strand | P11884 |
| I, K | Aldehyde dehydrogenase (EC 1.2.1.3) | protein | 11 | 64% helix, 0% strand | P11884 |
| J, L | Aldehyde dehydrogenase (EC 1.2.1.3) | protein | 13 | 62% helix, 0% strand | P11884 |
| M | Aldehyde dehydrogenase (EC 1.2.1.3) | protein | 7 | 0% helix, 0% strand | P11884 |
| N | Aldehyde dehydrogenase (EC 1.2.1.3) | protein | 9 | 67% helix, 0% strand | P11884 |
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 854 | 0.74 | 0.78 | 83 | empty |
| 2 | 119 | 0.38 | 0.74 | 18 | empty |
| 3 | 77 | 0.36 | 0.76 | 13 | empty |
| 4 | 66 | 0.31 | 0.74 | 13 | empty |
Interfaces
25 interfaces between chains.
- C–D · 545 Ų buried · 3 hydrogen bonds · protein-protein
- A–H · 497 Ų buried · 4 hydrogen bonds · protein-protein
- C–J · 495 Ų buried · 4 hydrogen bonds · protein-protein
- E–L · 495 Ų buried · 3 hydrogen bonds · protein-protein
- E–F · 477 Ų buried · 5 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 modified (nonstandard).
Compared structures
- 2V1S · Crystal structure of rat TOM20-aldh presequence complex · the same entry in another collection · chain K against K, TM-score 1.00
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt Q62760
- Every structure of UniProt P11884
- Elsewhere: RCSB PDB 2V1S · PDBe 2V1S · UniProt Q62760 · UniProt P11884
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