MolNFT v1 · #69353 · protein
Cystal structure of thermosome from acidianus tengchongensis strain S5
3KO1 · Chaperonin: “Cystal structure of thermosome from acidianus tengchongensis strain S5”. X-ray diffraction, 1 ligand (ADP), 20 pockets (best druggability 0.80). MolNFT v1 #69353 on GenesisL1: 3D structure, binding sites and pockets in…
- PDB
- 3KO1
- Type
- protein
- Length
- 4,545 residues
- Chains
- 9
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Chaperonin
- UniProt
- Q877H2
- Ligands
- ADP
- Pockets
- 20 · best druggability 0.80
Structure
x-ray diffraction · 1 distinct chain · 50% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G, H, I | Chaperonin | protein | 505 | 50% helix, 14% strand | Q877H2 |
Ligands and binding sites
- ADP · Adenosine-5'-diphosphate · ligand · 9 copies · chains A, B, C, D, E, F, G, H, I
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 12 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 956 | 0.80 | 0.82 | 95 | ADP |
| 2 | 1004 | 0.80 | 0.82 | 99 | ADP |
| 3 | 976 | 0.80 | 0.81 | 89 | ADP |
| 4 | 917 | 0.79 | 0.82 | 88 | ADP |
| 5 | 908 | 0.79 | 0.81 | 85 | ADP |
Interfaces
9 interfaces between chains.
- E–F · 998 Ų buried · 12 hydrogen bonds · protein-protein
- F–G · 997 Ų buried · 14 hydrogen bonds · protein-protein
- D–E · 974 Ų buried · 14 hydrogen bonds · protein-protein
- A–I · 959 Ų buried · 12 hydrogen bonds · protein-protein
- A–B · 941 Ų buried · 15 hydrogen bonds · protein-protein
Compared structures
- 3KO1 · Cystal structure of thermosome from Acidianus tengchongensis strain S5 · the same entry in another collection · chain D against D, 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 Q877H2
- Elsewhere: RCSB PDB 3KO1 · PDBe 3KO1 · UniProt Q877H2
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