Research workbench
Crystal structure of the bacterial fatty acid transporter fadl from escherichia COLI
Analyse Crystal structure of the bacterial fatty acid transporter fadl from escherichia… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1T16
- Type
- protein
- Length
- 854 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Long-chain fatty acid transport protein
- UniProt
- P10384
- Ligands
- CU
- Pockets
- 9 · best druggability 0.81
Structure
x-ray diffraction · 1 distinct chain · 12% helix, 53% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Long-chain fatty acid transport protein | protein | 427 | 12% helix, 53% strand | P10384 |
Ligands and binding sites
- CU · Copper (II) ion · metal · 6 copies · chains A, B
- LDA · Lauryl dimethylamine-N-oxide · additive · 4 copies · chains A, B
- C8E · (hydroxyethyloxy)tri(ethyloxy)octane · additive · 3 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
9 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 155 | 0.81 | 0.97 | 30 | LDA |
| 2 | 406 | 0.80 | 0.89 | 52 | LDA |
| 3 | 132 | 0.79 | 0.96 | 29 | LDA |
| 4 | 397 | 0.78 | 0.87 | 50 | LDA |
| 5 | 1069 | 0.72 | 0.75 | 96 | C8E |
Interfaces
1 interface between chains.
- A–B · 427 Ų buried · 6 hydrogen bonds · protein-protein
Compared structures
- 1T16 · Crystal structure of the bacterial fatty acid transporter FadL from Escherichia coli · the same entry in another collection · chain A against A, TM-score 1.00
- P10384 · AlphaFold monomer V2.0 prediction for long-chain fatty acid transport protein (P10384) · 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 P10384
- Elsewhere: RCSB PDB 1T16 · PDBe 1T16 · UniProt P10384
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