Research workbench
Focus classification structure of the hyperactive clpb mutant K476C, bound to casein, pre-state
Analyse Focus classification structure of the hyperactive clpb mutant K476C, bound to… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6OG1
- Type
- protein
- Length
- 1,152 residues
- Chains
- 2
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hyperactive disaggregase clpb
- Ligands
- ADP, AGS
- Pockets
- 20 · best druggability 0.87
Structure
electron microscopy · 2 distinct chains · 31% helix, 7% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| F | Hyperactive disaggregase clpb | protein | 571 | 27% helix, 4% strand | — |
| A | Hyperactive disaggregase clpb | protein | 581 | 34% helix, 10% strand | — |
Ligands and binding sites
- ADP · Adenosine-5'-diphosphate · ligand · 3 copies · chains F, A
- AGS · Phosphothiophosphoric acid-adenylate ester · ligand · chains F, A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 13 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 900 | 0.87 | 0.88 | 103 | empty |
| 2 | 1035 | 0.82 | 0.83 | 94 | AGS |
| 3 | 492 | 0.78 | 0.85 | 47 | empty |
| 4 | 198 | 0.76 | 0.91 | 28 | empty |
| 5 | 315 | 0.72 | 0.85 | 46 | empty |
Interfaces
1 interface between chains.
- F–A · 1891 Ų buried · 33 hydrogen bonds · protein-protein
Compared structures
- 6OG1 · Focus classification structure of the hyperactive ClpB mutant K476C, bound to casein… · 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
- Elsewhere: RCSB PDB 6OG1 · PDBe 6OG1
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