MolNFT v1 · #69625 · protein
Structural basis of the activity and substrate specificity of the fluoroacetyl-CoA thiesterase flk - wild type flk in complex with faccpan
3KVZ · Fluoroacetyl-CoA thioesterase flk: “Structural basis of the activity and substrate specificity of the fluoroacetyl-CoA thiesterase flk - wild…”. X-ray diffraction, 1 ligand (ENV), 18 pockets (best druggability 0.79). MolNFT v1…
- PDB
- 3KVZ
- Type
- protein
- Length
- 1,064 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Fluoroacetyl-CoA thioesterase flk
- EC
- 3.-.-.-
- UniProt
- Q1EMV2
- Ligands
- ENV
- Pockets
- 18 · best druggability 0.79
Structure
x-ray diffraction · 1 distinct chain · 26% helix, 40% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G, H | Fluoroacetyl-CoA thioesterase flk (EC 3.-.-.-) | protein | 133 | 26% helix, 40% strand | Q1EMV2 |
Ligands and binding sites
- ENV · (2R)-N-{3-[(5-fluoro-4-oxopentyl)amino]-3-oxopropyl}-2,4-dihydroxy-3,3-dimethylbutanamide · ligand · 2 copies · chains A, B, E, F
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
18 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 768 | 0.79 | 0.83 | 117 | empty |
| 2 | 517 | 0.69 | 0.79 | 64 | empty |
| 3 | 422 | 0.68 | 0.80 | 66 | ENV |
| 4 | 61 | 0.68 | 0.96 | 25 | empty |
| 5 | 328 | 0.66 | 0.81 | 55 | ENV |
Interfaces
13 interfaces between chains.
- A–B · 2059 Ų buried · 25 hydrogen bonds · protein-protein
- G–H · 2036 Ų buried · 26 hydrogen bonds · protein-protein
- E–F · 2032 Ų buried · 28 hydrogen bonds · protein-protein
- C–D · 2021 Ų buried · 25 hydrogen bonds · protein-protein
- C–H · 403 Ų buried · 5 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 disulfide (disulfide).
Compared structures
- 3KVZ · Structural basis of the activity and substrate specificity of the fluoroacetyl-CoA… · 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 3KVZ · PDBe 3KVZ · UniProt Q1EMV2
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