Research workbench
AlphaFold monomer V2.0 prediction for fatty acid-binding protein 5 (Q05816)
Analyse AlphaFold monomer V2.0 prediction for fatty acid-binding protein 5 (Q05816) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q05816
- Type
- protein
- Length
- 135 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x4b19F45398b689D52b4aF7DC26b26B77cd98f820
- UniProt
- Q05816
Structure
1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 135 | — | Q05816 |
Compared structures
- 4AZQ · Murine epidermal fatty acid-binding protein (FABP5) in complex with the endocannabinoid… · an experimental structure of the same protein · chain A against A, TM-score 0.99
- 4AZQ · Murine epidermal fatty acid-binding protein (FABP5) in complex with the endocannabinoid… · an experimental structure of the same protein · chain A against A, TM-score 0.99
- 7FYW · Crystal Structure of apo mouse FABP5, twinned in P21 with beta=90deg · an experimental structure of the same protein · chain A against B, TM-score 0.97
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 Q05816
- Elsewhere: UniProt Q05816 · AlphaFold DB Q05816
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