Research workbench
E. COLI aerobic trifunctional enzyme subunit-alpha
Analyse E. COLI aerobic 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
- 6TNM
- Type
- protein
- Length
- 719 residues
- Chains
- 1
- 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, 5.3.3.8, 1.1.1.35
- UniProt
- P21177
- Ligands
- ATP, NO3
- Pockets
- 5 · best druggability 0.74
Structure
x-ray diffraction · 1 distinct chain · 52% helix, 12% 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, 5.3.3.8, 1.1.1.35) | protein | 719 | 52% helix, 12% strand | P21177 |
Ligands and binding sites
- ATP · Adenosine-5'-triphosphate · ligand · chains A
- NO3 · Nitrate ion · ion · 7 copies · chains A
- GOL · Glycerol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 595 | 0.74 | 0.81 | 68 | NO3 |
| 2 | 446 | 0.66 | 0.78 | 72 | GOL, NO3 |
| 3 | 209 | 0.51 | 0.76 | 28 | empty |
| 4 | 50 | 0.43 | 0.84 | 18 | empty |
| 5 | 106 | 0.35 | 0.73 | 19 | NO3 |
Compared structures
- 6TNM · E. coli aerobic trifunctional enzyme subunit-alpha · the same entry in another collection · chain A against A, TM-score 1.00
- P21177 · AlphaFold monomer V2.0 prediction for fatty acid oxidation complex subunit alpha (P21177) · a predicted model 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 P21177
- Elsewhere: RCSB PDB 6TNM · PDBe 6TNM · UniProt P21177
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