Research workbench
AlphaFold monomer V2.0 prediction for HSP70-binding protein 1 (Q9NZL4)
Analyse AlphaFold monomer V2.0 prediction for HSP70-binding protein 1 (Q9NZL4) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q9NZL4
- Type
- protein
- Length
- 359 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x9377360E5534e0b32ED177Ed6f54ffBbf020C961
- UniProt
- Q9NZL4
Structure
1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 359 | — | Q9NZL4 |
Compared structures
- 1XQR · Crystal structure of the HSPBP1 core domain · an experimental structure of the same protein · chain A against A, TM-score 0.73
- 1XQR · Crystal structure of the HspBP1 core domain · an experimental structure of the same protein · chain A against A, TM-score 0.73
- 8X87 · The Crystal Structure of HspBP1 from Biortus. · an experimental structure of the same protein · chain A against A, TM-score 0.73
- 1XQS · Crystal structure of the HSPBP1 core domain complexed with the fragment of HSP70 ATPase… · an experimental structure of the same protein · chain A against A, TM-score 0.70
- 1XQS · Crystal structure of the HspBP1 core domain complexed with the fragment of Hsp70 ATPase… · an experimental structure of the same protein · chain A against A, TM-score 0.70
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 Q9NZL4
- Elsewhere: UniProt Q9NZL4 · AlphaFold DB Q9NZL4
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