Research workbench
Focus classification structure of the hyperactive clpb mutant K476C, bound to casein, ntd-trimer
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
- 6OG3
- Type
- protein
- Length
- 405 residues
- Chains
- 4
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hyperactive disaggregase clpb; Alpha S1-casein
- UniProt
- P63284
- Pockets
- 3 · best druggability 0.53
Structure
electron microscopy · 2 distinct chains · 0% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| E, C, A | Hyperactive disaggregase clpb | protein | 132 | 0% helix, 0% strand | P63284 |
| P | Alpha S1-casein | protein | 9 | 0% helix, 0% strand | — |
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 372 | 0.53 | 0.73 | 62 | empty |
| 2 | 311 | 0.50 | 0.73 | 58 | empty |
| 3 | 287 | 0.49 | 0.73 | 53 | empty |
Interfaces
3 interfaces between chains.
- C–A · 33 Ų buried · 0 hydrogen bonds · protein-protein
- E–P · 20 Ų buried · 0 hydrogen bonds · protein-protein
- E–C · 16 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 6OG3 · Focus classification structure of the hyperactive ClpB mutant K476C, bound to casein… · the same entry in another collection · chain E against E, TM-score 1.00
- P63284 · AlphaFold monomer V2.0 prediction for chaperone protein clpb (P63284) · a predicted model of the same protein · chain C against A, TM-score 0.99
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 P63284
- Elsewhere: RCSB PDB 6OG3 · PDBe 6OG3 · UniProt P63284
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