Research workbench
Mtb clpb in complex with amppnp
Analyse Mtb clpb in complex with amppnp in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6ED3
- Type
- protein
- Length
- 3,192 residues
- Chains
- 6
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Chaperone protein clpb
- UniProt
- P9WPD0
- Pockets
- 20 · best druggability 0.55
Structure
electron microscopy · 1 distinct chain · 38% helix, 10% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F | Chaperone protein clpb | protein | 532 | 38% helix, 10% strand | P9WPD0 |
Pockets
20 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 444 | 0.55 | 0.73 | 60 | empty |
| 2 | 488 | 0.54 | 0.72 | 70 | empty |
| 3 | 414 | 0.53 | 0.73 | 56 | empty |
| 4 | 447 | 0.53 | 0.72 | 74 | empty |
| 5 | 419 | 0.52 | 0.72 | 61 | empty |
Interfaces
5 interfaces between chains.
- B–C · 274 Ų buried · 3 hydrogen bonds · protein-protein
- C–D · 267 Ų buried · 3 hydrogen bonds · protein-protein
- D–E · 236 Ų buried · 3 hydrogen bonds · protein-protein
- A–B · 230 Ų buried · 1 hydrogen bond · protein-protein
- A–F · 214 Ų buried · 2 hydrogen bonds · protein-protein
Compared structures
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 P9WPD0
- Elsewhere: RCSB PDB 6ED3 · PDBe 6ED3 · UniProt P9WPD0
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