MolNFT v1 · #163900 · protein
Structure of the APO2 state of the heptameric BCS1 aaa-ATPase
6SH5 · Mitochondrial chaperone BCS1: “Structure of the APO2 state of the heptameric BCS1 aaa-ATPase”. Electron microscopy, 20 pockets (best druggability 0.76). MolNFT v1 #163900 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6SH5
- Type
- protein
- Length
- 2,338 residues
- Chains
- 7
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Mitochondrial chaperone BCS1
- UniProt
- P32839
- Pockets
- 20 · best druggability 0.76
Structure
electron microscopy · 1 distinct chain · 35% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G | Mitochondrial chaperone BCS1 | protein | 334 | 35% 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 | 904 | 0.76 | 0.80 | 131 | empty |
| 2 | 803 | 0.76 | 0.80 | 112 | empty |
| 3 | 822 | 0.76 | 0.80 | 117 | empty |
| 4 | 809 | 0.76 | 0.80 | 125 | empty |
| 5 | 695 | 0.74 | 0.80 | 98 | empty |
Interfaces
7 interfaces between chains.
- A–B · 330 Ų buried · 0 hydrogen bonds · protein-protein
- B–C · 325 Ų buried · 0 hydrogen bonds · protein-protein
- D–E · 321 Ų buried · 0 hydrogen bonds · protein-protein
- E–F · 321 Ų buried · 0 hydrogen bonds · protein-protein
- C–D · 320 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 6SH5 · Structure of the Apo2 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 F against A, TM-score 0.75
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 6SH5 · PDBe 6SH5 · UniProt P32839
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