Research workbench
E. COLI anaerobic trifunctional enzyme subunit-alpha
Analyse E. COLI anaerobic trifunctional enzyme subunit-alpha in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6YSV
- Type
- protein
- Length
- 1,407 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Fatty acid oxidation complex subunit alpha
- EC
- 4.2.1.17, 5.1.2.3, 1.1.1.35
- UniProt
- P77399
- Ligands
- SO4
- Pockets
- 13 · best druggability 0.80
Structure
x-ray diffraction · 2 distinct chains · 50% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Fatty acid oxidation complex subunit alpha (EC 4.2.1.17, 5.1.2.3, 1.1.1.35) | protein | 708 | 51% helix, 11% strand | P77399 |
| B | Fatty acid oxidation complex subunit alpha (EC 4.2.1.17, 5.1.2.3, 1.1.1.35) | protein | 699 | 49% helix, 11% strand | P77399 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 7 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
13 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 605 | 0.80 | 0.85 | 89 | SO4 |
| 2 | 1103 | 0.79 | 0.80 | 129 | SO4 |
| 3 | 396 | 0.71 | 0.82 | 47 | empty |
| 4 | 436 | 0.58 | 0.74 | 51 | empty |
| 5 | 194 | 0.48 | 0.75 | 27 | empty |
Interfaces
1 interface between chains.
- A–B · 241 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 6YSV · E. coli anaerobic trifunctional enzyme subunit-alpha · the same entry in another collection · chain A against A, TM-score 1.00
- P77399 · AlphaFold monomer V2.0 prediction for fatty acid oxidation complex subunit alpha (P77399) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 P77399
- Elsewhere: RCSB PDB 6YSV · PDBe 6YSV · UniProt P77399
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