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AlphaFold monomer V2.0 prediction for lipoamide acyltransferase component of branched-chain alpha-keto acid dehydrogenase complex, mitochondrial (P53395)
Analyse AlphaFold monomer V2.0 prediction for lipoamide acyltransferase component of… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P53395
- Type
- protein
- Length
- 482 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x010B024D599893c4b5edc91b70cCb2Dc2F8A321a
- Molecule
- Lipoamide acyltransferase component of branched-chain alpha-keto acid dehydrogenase…
- UniProt
- P53395
- Pockets
- 4 · best druggability 0.52
Structure
1 distinct chain · 24% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Lipoamide acyltransferase component of branched-chain alpha-keto acid dehydrogenase complex, mitochondrial | protein | 482 | 24% helix, 22% strand | P53395 |
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 221 | 0.52 | 0.76 | 29 | empty |
| 2 | 209 | 0.50 | 0.76 | 29 | empty |
| 3 | 109 | 0.42 | 0.76 | 16 | empty |
| 4 | 54 | 0.30 | 0.76 | 13 | empty |
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 P53395
- Elsewhere: UniProt P53395 · AlphaFold DB P53395
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