Research workbench
Crystal structure of csaa chaperone protein from picrophilus torridus
Analyse Crystal structure of csaa chaperone protein from picrophilus torridus in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5ZDI
- Type
- protein
- Length
- 214 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein secretion chaperonin csaa
- UniProt
- Q6L208
- Pockets
- 2 · best druggability 0.48
Structure
x-ray diffraction · 1 distinct chain · 12% helix, 46% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Protein secretion chaperonin csaa | protein | 107 | 12% helix, 46% strand | Q6L208 |
Ligands and binding sites
- GOL · Glycerol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 131 | 0.48 | 0.78 | 25 | empty |
| 2 | 138 | 0.47 | 0.77 | 22 | empty |
Interfaces
1 interface between chains.
- A–B · 1648 Ų buried · 19 hydrogen bonds · protein-protein
Compared structures
- 5ZDI · Crystal structure of CsaA chaperone protein from picrophilus torridus · the same entry in another collection · chain A against A, 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
- Every structure of UniProt Q6L208
- Elsewhere: RCSB PDB 5ZDI · PDBe 5ZDI · UniProt Q6L208
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