Research workbench
Structure of the APO1 state of the heptameric BCS1 aaa-ATPase.
Analyse Structure of the APO1 state of the heptameric BCS1 aaa-ATPase. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6SH4
- Type
- protein
- Length
- 2,632 residues
- Chains
- 7
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Mitochondrial chaperone BCS1
- UniProt
- P32839
- Pockets
- 20 · best druggability 0.78
Structure
electron microscopy · 1 distinct chain · 38% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G | Mitochondrial chaperone BCS1 | protein | 376 | 38% helix, 24% strand | P32839 |
Pockets
20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 999 | 0.78 | 0.80 | 132 | empty |
| 2 | 995 | 0.78 | 0.80 | 126 | empty |
| 3 | 972 | 0.78 | 0.80 | 129 | empty |
| 4 | 689 | 0.74 | 0.80 | 90 | empty |
| 5 | 669 | 0.74 | 0.80 | 86 | empty |
Interfaces
7 interfaces between chains.
- F–G · 626 Ų buried · 2 hydrogen bonds · protein-protein
- B–C · 612 Ų buried · 2 hydrogen bonds · protein-protein
- E–F · 601 Ų buried · 1 hydrogen bond · protein-protein
- A–G · 589 Ų buried · 1 hydrogen bond · protein-protein
- A–B · 579 Ų buried · 1 hydrogen bond · protein-protein
Compared structures
- 6SH4 · Structure of the Apo1 state of the heptameric Bcs1 AAA-ATPase. · the same entry in another collection · chain G against G, TM-score 1.00
- P32839 · AlphaFold monomer V2.0 prediction for mitochondrial chaperone BCS1 (P32839) · a predicted model of the same protein · chain D against A, TM-score 0.66
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 P32839
- Elsewhere: RCSB PDB 6SH4 · PDBe 6SH4 · UniProt P32839
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