Research workbench
NMR structure of the substrate binding domain of dnak, 25 structures
Analyse NMR structure of the substrate binding domain of dnak, 25 structures in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2BPR
- Type
- protein
- Length
- 173 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Dnak
- UniProt
- P0A6Y8
- Pockets
- 3 · best druggability 0.35
Structure
solution nmr · 1 distinct chain · 13% helix, 35% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Dnak | protein | 173 | 13% helix, 35% strand | P0A6Y8 |
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 104 | 0.35 | 0.74 | 18 | empty |
| 2 | 59 | 0.31 | 0.76 | 23 | empty |
| 3 | 53 | 0.30 | 0.76 | 12 | empty |
Compared structures
- 2BPR · NMR structure of the substrate binding domain of dnak, 25 structures · the same entry in another collection · chain A against A, TM-score 1.00
- P0A6Y8 · AlphaFold monomer V2.0 prediction for chaperone protein dnak (P0A6Y8) · a predicted model of the same protein · chain A against A, TM-score 0.54
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 P0A6Y8
- Elsewhere: RCSB PDB 2BPR · PDBe 2BPR · UniProt P0A6Y8
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