MolNFT v1 · #59361 · protein
Crystal structure of human co-chaperone protein hscb
3BVO · Co-chaperone protein hscb, mitochondrial precursor: “Crystal structure of human co-chaperone protein hscb”. X-ray diffraction, 2 ligands (ZN, SO4), 6 pockets (best druggability 0.53). MolNFT v1 #59361 on GenesisL1: 3D structure…
- PDB
- 3BVO
- Type
- protein
- Length
- 374 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Co-chaperone protein hscb, mitochondrial precursor
- UniProt
- Q8IWL3
- Ligands
- ZN, SO4
- Pockets
- 6 · best druggability 0.53
Structure
x-ray diffraction · 2 distinct chains · 65% helix, 2% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Co-chaperone protein hscb, mitochondrial precursor | protein | 197 | 62% helix, 2% strand | Q8IWL3 |
| B | Co-chaperone protein hscb, mitochondrial precursor | protein | 177 | 68% helix, 1% strand | Q8IWL3 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 50 | 0.53 | 0.89 | 15 | empty |
| 2 | 163 | 0.50 | 0.78 | 27 | empty |
| 3 | 60 | 0.48 | 0.85 | 15 | empty |
| 4 | 113 | 0.37 | 0.74 | 19 | empty |
| 5 | 54 | 0.31 | 0.77 | 11 | empty |
Interfaces
1 interface between chains.
- A–B · 595 Ų buried · 12 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 10 modified (engineered).
Compared structures
- 3BVO · Crystal structure of human co-chaperone protein HscB · the same entry in another collection · chain A against A, TM-score 1.00
- Q8IWL3 · AlphaFold monomer V2.0 prediction for iron-sulfur cluster co- chaperone protein hscb… · a predicted model of the same protein · chain A against A, TM-score 0.95
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 Q8IWL3
- Elsewhere: RCSB PDB 3BVO · PDBe 3BVO · UniProt Q8IWL3
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