MolNFT v1 · #9430 · protein
HSP33, heat shock protein with redox-regulated chaperone activity
1HW7 · Heat shock protein HSP33: “HSP33, heat shock protein with redox-regulated chaperone activity”. X-ray diffraction, 2 ligands (ZN, SO4), 1 pocket (best druggability 0.49). MolNFT v1 #9430 on GenesisL1: 3D structure, binding sites and…
- PDB
- 1HW7
- Type
- protein
- Length
- 229 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Heat shock protein HSP33
- UniProt
- P0A6Y5
- Ligands
- ZN, SO4
- Pockets
- 1 · best druggability 0.49
Structure
x-ray diffraction · 1 distinct chain · 31% helix, 31% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Heat shock protein HSP33 | protein | 229 | 31% helix, 31% strand | P0A6Y5 |
Ligands and binding sites
- ZN · Zinc ion · metal · chains A
- SO4 · Sulfate ion · ion · 4 copies · chains A
- MES · 2-(N-morpholino)-ethanesulfonic acid · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 179 | 0.49 | 0.76 | 19 | MES |
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 P0A6Y5
- Elsewhere: RCSB PDB 1HW7 · PDBe 1HW7 · UniProt P0A6Y5
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