Research workbench
AlphaFold monomer V2.0 prediction for propionyl-CoA carboxylase alpha chain, mitochondrial (P05165)
Analyse AlphaFold monomer V2.0 prediction for propionyl-CoA carboxylase alpha chain… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P05165
- Type
- protein
- Length
- 728 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xb4D2d9c96b0D792d0b77e7147D724cc1F801ae58
- Molecule
- Propionyl-CoA carboxylase alpha chain, mitochondrial
- UniProt
- P05165
- Pockets
- 5 · best druggability 0.79
Structure
1 distinct chain · 26% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Propionyl-CoA carboxylase alpha chain, mitochondrial | protein | 728 | 26% helix, 30% strand | P05165 |
Pockets
5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 953 | 0.79 | 0.81 | 95 | empty |
| 2 | 295 | 0.54 | 0.76 | 27 | empty |
| 3 | 74 | 0.36 | 0.77 | 15 | empty |
| 4 | 59 | 0.30 | 0.75 | 13 | empty |
| 5 | 78 | 0.30 | 0.73 | 17 | empty |
Compared structures
- 8XL5 · Structure of human propionyl-CoA carboxylase in complex with propionyl-CoA (PCC-PCO) · an experimental structure of the same protein · chain A against A, TM-score 0.79
- 8XL4 · Structure of human propionyl-CoA carboxylase in complex with acetyl-CoA (PCC-ACO) · an experimental structure of the same protein · chain A against I, TM-score 0.79
- 8XL3 · Structure of human propionyl-CoA carboxylase at apo-state (PCC-Apo) · an experimental structure of the same protein · chain A against E, TM-score 0.78
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 P05165
- Elsewhere: UniProt P05165 · AlphaFold DB P05165
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