Research workbench
Crystal structure of the dnak C-terminus (dnak-sbd-B)
Analyse Crystal structure of the dnak C-terminus (dnak-sbd-B) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4R5K
- Type
- protein
- Length
- 444 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Chaperone protein dnak
- UniProt
- P0A6Y8
- Ligands
- CA, SO4
- Pockets
- 5 · best druggability 0.69
Structure
x-ray diffraction · 2 distinct chains · 41% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Chaperone protein dnak | protein | 221 | 41% helix, 29% strand | P0A6Y8 |
| B | Chaperone protein dnak | protein | 223 | 42% helix, 27% strand | P0A6Y8 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 638 | 0.69 | 0.78 | 82 | empty |
| 2 | 126 | 0.45 | 0.77 | 21 | empty |
| 3 | 69 | 0.44 | 0.81 | 15 | empty |
| 4 | 101 | 0.34 | 0.73 | 17 | SO4 |
| 5 | 54 | 0.32 | 0.77 | 11 | empty |
Interfaces
1 interface between chains.
- A–B · 1830 Ų buried · 30 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 P0A6Y8
- Elsewhere: RCSB PDB 4R5K · PDBe 4R5K · UniProt P0A6Y8
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