Research workbench
AlphaFold monomer V2.0 prediction for propionyl-CoA carboxylase beta chain, mitochondrial (P05166)
Analyse AlphaFold monomer V2.0 prediction for propionyl-CoA carboxylase beta chain… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P05166
- Type
- protein
- Length
- 539 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x79a905d858Ce72991FD6E7a9C6498620f42E146D
- Molecule
- Propionyl-CoA carboxylase beta chain, mitochondrial
- UniProt
- P05166
- Pockets
- 3 · best druggability 0.58
Structure
1 distinct chain · 45% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Propionyl-CoA carboxylase beta chain, mitochondrial | protein | 539 | 45% helix, 18% strand | P05166 |
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 350 | 0.58 | 0.76 | 43 | empty |
| 2 | 135 | 0.47 | 0.78 | 27 | empty |
| 3 | 57 | 0.29 | 0.74 | 15 | empty |
Compared structures
- 7YBU · Human propionyl-coenzyme A carboxylase · an experimental structure of the same protein · chain A against P, TM-score 0.93
- 8XL5 · Structure of human propionyl-CoA carboxylase in complex with propionyl-CoA (PCC-PCO) · an experimental structure of the same protein · chain A against L, TM-score 0.93
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 P05166
- Elsewhere: UniProt P05166 · AlphaFold DB P05166
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