MolNFT v1 · #69627 · protein
Structural basis of the activity and substrate specificity of the fluoroacetyl-CoA flk - wild type flk in complex with facopan
3KW1 · Fluoroacetyl-CoA thioesterase: “Structural basis of the activity and substrate specificity of the fluoroacetyl-CoA flk - wild type flk in…”. X-ray diffraction, 1 ligand (ENW), 15 pockets (best druggability 0.75). MolNFT v1 #69627 on…
- PDB
- 3KW1
- Type
- protein
- Length
- 1,064 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Fluoroacetyl-CoA thioesterase
- EC
- 3.-.-.-
- UniProt
- Q1EMV2
- Ligands
- ENW
- Pockets
- 15 · best druggability 0.75
Structure
x-ray diffraction · 1 distinct chain · 29% helix, 41% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G, H | Fluoroacetyl-CoA thioesterase (EC 3.-.-.-) | protein | 133 | 29% helix, 41% strand | Q1EMV2 |
Ligands and binding sites
- ENW · 2-({N-[(2S)-2,4-dihydroxy-3,3-dimethylbutanoyl]-beta-alanyl}amino)ethyl fluoroacetate · ligand · 2 copies · chains C, D, E, F
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
15 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 806 | 0.75 | 0.80 | 110 | ENW |
| 2 | 700 | 0.73 | 0.80 | 105 | ENW |
| 3 | 578 | 0.70 | 0.79 | 63 | empty |
| 4 | 319 | 0.67 | 0.82 | 44 | empty |
| 5 | 155 | 0.56 | 0.81 | 33 | empty |
Interfaces
13 interfaces between chains.
- A–B · 2075 Ų buried · 26 hydrogen bonds · protein-protein
- C–D · 2054 Ų buried · 27 hydrogen bonds · protein-protein
- E–F · 2046 Ų buried · 26 hydrogen bonds · protein-protein
- G–H · 2042 Ų buried · 27 hydrogen bonds · protein-protein
- D–G · 441 Ų buried · 3 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 disulfide (disulfide).
Compared structures
- 3KW1 · Structural basis of the activity and substrate specificity of the fluoroacetyl-CoA FlK… · the same entry in another collection · chain H against H, TM-score 1.00
- Q1EMV2 · AlphaFold monomer V2.0 prediction for fluoroacetyl-CoA thioesterase (Q1EMV2) · a predicted model of the same protein · chain F 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 Q1EMV2
- Elsewhere: RCSB PDB 3KW1 · PDBe 3KW1 · UniProt Q1EMV2
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