MolNFT v1 · #69585 · protein
Structural basis of the activity and substrate specificity of the fluoroacetyl-CoA thioesterase flk - T42S mutant in complex with acetate.
3KUV · Fluoroacetyl coenzyme a thioesterase: “Structural basis of the activity and substrate specificity of the fluoroacetyl-CoA thioesterase flk - T42S…”. X-ray diffraction, 3 pockets (best druggability 0.62). MolNFT v1 #69585 on…
- PDB
- 3KUV
- Type
- protein
- Length
- 265 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Fluoroacetyl coenzyme a thioesterase
- EC
- 3.-.-.-
- UniProt
- Q1EMV2
- Pockets
- 3 · best druggability 0.62
Structure
x-ray diffraction · 2 distinct chains · 29% helix, 41% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Fluoroacetyl coenzyme a thioesterase (EC 3.-.-.-) | protein | 132 | 28% helix, 41% strand | Q1EMV2 |
| B | Fluoroacetyl coenzyme a thioesterase (EC 3.-.-.-) | protein | 133 | 31% helix, 41% strand | Q1EMV2 |
Ligands and binding sites
- ACT · Acetate ion · additive · 7 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 111 | 0.62 | 0.87 | 28 | ACT |
| 2 | 226 | 0.61 | 0.81 | 44 | ACT |
| 3 | 53 | 0.40 | 0.81 | 13 | empty |
Interfaces
1 interface between chains.
- A–B · 2018 Ų buried · 28 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 3KUV · 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 3KUV · PDBe 3KUV · UniProt Q1EMV2
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