MolNFT v1 · #69608 · protein
Structural basis of the activity and substrate specificity of the fluoroacetyl-CoA thioesterase flk - T42A mutant in complex with fluoro-acetate
3KVI: “Structural basis of the activity and substrate specificity of the fluoroacetyl-CoA thioesterase flk - T42A…”. X-ray diffraction, 1 ligand (FAH), 2 pockets (best druggability 0.68). MolNFT v1 #69608 on GenesisL1: 3D structure…
- PDB
- 3KVI
- Type
- protein
- Length
- 266 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Fluoroacetyl-CoA thioesterase flk
- EC
- 3.-.-.-
- UniProt
- Q1EMV2
- Ligands
- FAH
- Pockets
- 2 · best druggability 0.68
Structure
x-ray diffraction · 1 distinct chain · 29% helix, 41% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Fluoroacetyl-CoA thioesterase flk (EC 3.-.-.-) | protein | 133 | 29% helix, 41% strand | Q1EMV2 |
Ligands and binding sites
- FAH · fluoroacetic acid · ligand · 4 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 243 | 0.68 | 0.84 | 41 | FAH |
| 2 | 107 | 0.56 | 0.84 | 29 | FAH |
Interfaces
1 interface between chains.
- A–B · 2043 Ų buried · 28 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 3KVI · Structural basis of the activity and substrate specificity of the fluoroacetyl-CoA… · the same entry in another collection · chain A against A, TM-score 1.00
- Q1EMV2 · AlphaFold monomer V2.0 prediction for fluoroacetyl-CoA thioesterase (Q1EMV2) · a predicted model of the same protein · chain B against A, TM-score 1.00
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 Q1EMV2
- Elsewhere: RCSB PDB 3KVI · PDBe 3KVI · UniProt Q1EMV2
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