Research workbench
AlphaFold monomer V2.0 prediction for heat shock protein 90 (Q18688)
Analyse AlphaFold monomer V2.0 prediction for heat shock protein 90 (Q18688) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q18688
- Type
- protein
- Length
- 702 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x864cA926416301AABc2d76b08077e6786c9F3707
- UniProt
- Q18688
Structure
1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 702 | — | Q18688 |
Compared structures
- 4GQT · N-terminal domain of C. elegans Hsp90 · an experimental structure of the same protein · chain A against A, TM-score 0.25
- 4GQT · N-terminal domain of C. elegans HSP90 · an experimental structure of the same protein · chain A against A, TM-score 0.25
- 4I2Z · Crystal structure of the myosin chaperone unc-45 from C.ELEGANS in complex with a HSP90… · an experimental structure of the same protein · chain A against B, TM-score 0.01
- 4I2Z · Crystal structure of the myosin chaperone UNC-45 from C.elegans in complex with a Hsp90… · an experimental structure of the same protein · chain A against B, TM-score 0.01
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 Q18688
- Elsewhere: UniProt Q18688 · AlphaFold DB Q18688
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