MolNFT v1 · #175094 · protein
Staggered ring conformation of CTHSP104 (HSP104 from chaetomium thermophilum)
7CG3 · Heat shock protein 104: “Staggered ring conformation of CTHSP104 (HSP104 from chaetomium thermophilum)”. Electron microscopy, 20 pockets (best druggability 0.87). MolNFT v1 #175094 on GenesisL1: 3D structure, binding sites and…
- PDB
- 7CG3
- Type
- protein
- Length
- 3,762 residues
- Chains
- 6
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Heat shock protein 104
- UniProt
- A0A2Z6G185
- Pockets
- 20 · best druggability 0.87
Structure
electron microscopy · 2 distinct chains · 54% helix, 8% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| F, A, B | Heat shock protein 104 | protein | 568 | 50% helix, 7% strand | A0A2Z6G185 |
| C, D, E | Heat shock protein 104 | protein | 686 | 58% helix, 9% strand | A0A2Z6G185 |
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 | 1033 | 0.87 | 0.88 | 136 | empty |
| 2 | 803 | 0.86 | 0.88 | 111 | empty |
| 3 | 1027 | 0.84 | 0.85 | 137 | empty |
| 4 | 1041 | 0.84 | 0.84 | 126 | empty |
| 5 | 1034 | 0.83 | 0.84 | 131 | empty |
Interfaces
6 interfaces between chains.
- D–E · 2157 Ų buried · 21 hydrogen bonds · protein-protein
- C–D · 2091 Ų buried · 24 hydrogen bonds · protein-protein
- F–A · 1799 Ų buried · 24 hydrogen bonds · protein-protein
- B–C · 1453 Ų buried · 21 hydrogen bonds · protein-protein
- A–B · 1428 Ų buried · 23 hydrogen bonds · protein-protein
Compared structures
- 7CG3 · Staggered ring conformation of CtHsp104 (Hsp104 from Chaetomium Thermophilum) · the same entry in another collection · chain F against F, 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 A0A2Z6G185
- Elsewhere: RCSB PDB 7CG3 · PDBe 7CG3 · UniProt A0A2Z6G185
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