Research workbench
AlphaFold monomer V2.0 prediction for putative polyketide biosynthesis enoyl-CoA isomerase pksi (P40802)
Analyse AlphaFold monomer V2.0 prediction for putative polyketide biosynthesis… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P40802
- Type
- protein
- Length
- 249 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x26D3C47A86831ff95e84759c65F671f9744Fa55e
- Molecule
- Putative polyketide biosynthesis enoyl-CoA isomerase pksi
- UniProt
- P40802
- Pockets
- 2 · best druggability 0.71
Structure
1 distinct chain · 50% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Putative polyketide biosynthesis enoyl-CoA isomerase pksi | protein | 249 | 50% helix, 19% strand | P40802 |
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 310 | 0.71 | 0.85 | 46 | empty |
| 2 | 85 | 0.34 | 0.74 | 18 | empty |
Compared structures
- 4Q1G · Structure and mechanism of a dehydratase/decarboxylase enzyme couple involved in… · an experimental structure of the same protein · chain A against B, TM-score 0.98
- 4Q1G · Structure and mechanism of a DEHYDRATASE/DECARBOXYLASE enzyme couple involved in… · an experimental structure of the same protein · chain A against B, TM-score 0.98
- 4Q1K · Structure and mechanism of a dehydratase/decarboxylase enzyme couple involved in… · an experimental structure of the same protein · chain A against C, TM-score 0.98
- 4Q1K · Structure and mechanism of a DEHYDRATASE/DECARBOXYLASE enzyme couple involved in… · an experimental structure of the same protein · chain A against C, TM-score 0.98
- 4Q1I · Structure and mechanism of a dehydratase/decarboxylase enzyme couple involved in… · an experimental structure of the same protein · chain A against B, TM-score 0.98
- 4Q1I · Structure and mechanism of a DEHYDRATASE/DECARBOXYLASE enzyme couple involved in… · an experimental structure of the same protein · chain A against B, TM-score 0.98
- 4Q1J · Structure and mechanism of a dehydratase/decarboxylase enzyme couple involved in… · an experimental structure of the same protein · chain A against A, TM-score 0.98
- 4Q1J · Structure and mechanism of a DEHYDRATASE/DECARBOXYLASE enzyme couple involved in… · an experimental structure of the same protein · chain A against A, TM-score 0.98
- 4Q1H · Structure and mechanism of a dehydratase/decarboxylase enzyme couple involved in… · an experimental structure of the same protein · chain A against A, TM-score 0.98
- 4Q1H · Structure and mechanism of a DEHYDRATASE/DECARBOXYLASE enzyme couple involved in… · an experimental structure of the same protein · chain A against A, TM-score 0.98
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 P40802
- Elsewhere: UniProt P40802 · AlphaFold DB P40802
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