MolNFT v1 · #173433 · protein
Structure of the human mitochondrial HSPD1 single ring
7AZP · 60 kda heat shock protein, mitochondrial: “Structure of the human mitochondrial HSPD1 single ring”. Electron microscopy, 20 pockets (best druggability 0.78). MolNFT v1 #173433 on GenesisL1: 3D structure, binding sites and pockets in…
- PDB
- 7AZP
- Type
- protein
- Length
- 3,675 residues
- Chains
- 7
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 60 kda heat shock protein, mitochondrial
- EC
- 5.6.1.7
- UniProt
- P10809
- Pockets
- 20 · best druggability 0.78
Structure
electron microscopy · 1 distinct chain · 51% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G | 60 kda heat shock protein, mitochondrial (EC 5.6.1.7) | protein | 525 | 51% helix, 18% strand | P10809 |
Pockets
20 pockets found on a 1 Å grid, 16 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1097 | 0.78 | 0.80 | 99 | empty |
| 2 | 880 | 0.77 | 0.80 | 87 | empty |
| 3 | 521 | 0.74 | 0.82 | 60 | empty |
| 4 | 401 | 0.73 | 0.84 | 51 | empty |
| 5 | 812 | 0.73 | 0.78 | 86 | empty |
Interfaces
7 interfaces between chains.
- B–C · 1324 Ų buried · 10 hydrogen bonds · protein-protein
- A–B · 1323 Ų buried · 8 hydrogen bonds · protein-protein
- C–D · 1310 Ų buried · 9 hydrogen bonds · protein-protein
- F–G · 1308 Ų buried · 7 hydrogen bonds · protein-protein
- E–F · 1302 Ų buried · 8 hydrogen bonds · protein-protein
Compared structures
- 7AZP · Structure of the human mitochondrial HSPD1 single ring · the same entry in another collection · chain G against G, TM-score 1.00
- P10809 · AlphaFold monomer V2.0 prediction for 60 kda heat shock protein, mitochondrial (P10809) · a predicted model of the same protein · chain B 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 P10809
- Elsewhere: RCSB PDB 7AZP · PDBe 7AZP · UniProt P10809
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