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Crystal structure of the bacillus subtilis HSP33
Analyse Crystal structure of the bacillus subtilis HSP33 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1VZY
- Type
- protein
- Length
- 576 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 33 kda chaperonin
- UniProt
- P37565
- Ligands
- ZN
- Pockets
- 5 · best druggability 0.72
Structure
x-ray diffraction · 2 distinct chains · 34% helix, 31% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 33 kda chaperonin | protein | 290 | 36% helix, 30% strand | P37565 |
| B | 33 kda chaperonin | protein | 286 | 33% helix, 31% strand | P37565 |
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 | 521 | 0.72 | 0.81 | 64 | empty |
| 2 | 230 | 0.47 | 0.74 | 34 | empty |
| 3 | 187 | 0.47 | 0.75 | 31 | empty |
| 4 | 65 | 0.33 | 0.76 | 14 | empty |
| 5 | 57 | 0.32 | 0.77 | 17 | empty |
Interfaces
1 interface between chains.
- A–B · 1270 Ų buried · 25 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 P37565
- Elsewhere: RCSB PDB 1VZY · PDBe 1VZY · UniProt P37565
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