Research workbench
Crystal structure of 33 kda chaperonin (heat shock protein 33 homolog) (HSP33) (TM1394) from thermotoga maritima at 2.20 a resolution
Analyse Crystal structure of 33 kda chaperonin (heat shock protein 33 homolog) (HSP33)… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1VQ0
- Type
- protein
- Length
- 580 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 33 kda chaperonin
- UniProt
- Q9X1B4
- Ligands
- UNL, ZN, CL
- Pockets
- 4 · best druggability 0.64
Structure
x-ray diffraction · 1 distinct chain · 36% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | 33 kda chaperonin | protein | 290 | 36% helix, 29% strand | Q9X1B4 |
Ligands and binding sites
- UNL · Unknown ligand · ligand · 2 copies · chains A, B
- ZN · Zinc ion · metal · 2 copies · chains A, B
- CL · Chloride ion · ion · 2 copies · chains A, B
- EDO · 1,2-ethanediol · additive · 3 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 248 | 0.64 | 0.82 | 35 | EDO |
| 2 | 231 | 0.50 | 0.75 | 39 | empty |
| 3 | 140 | 0.40 | 0.74 | 23 | empty |
| 4 | 73 | 0.36 | 0.76 | 16 | empty |
Interfaces
1 interface between chains.
- A–B · 686 Ų buried · 8 hydrogen bonds · protein-protein
Compared structures
- 1VQ0 · Crystal structure of 33 kDa chaperonin (Heat shock protein 33 homolog) (HSP33) (TM1394)… · the same entry in another collection · chain A against A, TM-score 1.00
- Q9X1B4 · AlphaFold monomer V2.0 prediction for 33 kda chaperonin (Q9X1B4) · a predicted model of the same protein · chain A against A, TM-score 0.98
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 Q9X1B4
- Elsewhere: RCSB PDB 1VQ0 · PDBe 1VQ0 · UniProt Q9X1B4
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