Research workbench
Crystal structure of the myosin chaperone unc-45 from C.ELEGANS in complex with a HSP90 peptide
Analyse Crystal structure of the myosin chaperone unc-45 from C.ELEGANS in complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4I2Z
- Type
- protein
- Length
- 907 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein unc-45; Heat shock protein 90
- UniProt
- G5EG62, Q18688
- Pockets
- 9 · best druggability 0.72
Structure
x-ray diffraction · 2 distinct chains · 66% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein unc-45 | protein | 899 | 66% helix, 0% strand | G5EG62 |
| B | Heat shock protein 90 | protein | 8 | 0% helix, 0% strand | Q18688 |
Pockets
9 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 846 | 0.72 | 0.77 | 78 | empty |
| 2 | 484 | 0.70 | 0.80 | 57 | empty |
| 3 | 722 | 0.68 | 0.76 | 54 | empty |
| 4 | 92 | 0.62 | 0.88 | 28 | empty |
| 5 | 131 | 0.49 | 0.79 | 23 | empty |
Interfaces
1 interface between chains.
- A–B · 609 Ų buried · 9 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 25 modified (engineered).
Compared structures
- 4I2Z · Crystal structure of the myosin chaperone UNC-45 from C.elegans in complex with a Hsp90… · the same entry in another collection · chain A against A, TM-score 1.00
- Q18688 · AlphaFold monomer V2.0 prediction for heat shock protein 90 (Q18688) · a predicted model of the same protein · chain B against A, TM-score 0.51
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 G5EG62
- Every structure of UniProt Q18688
- Elsewhere: RCSB PDB 4I2Z · PDBe 4I2Z · UniProt G5EG62 · UniProt Q18688
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