Research workbench
Crystal structure of the F36A mutant of the fluoroacetyl-CoA-specific thioesterase flk in complex with fluoroacetate and CoA
Analyse Crystal structure of the F36A mutant of the fluoroacetyl-CoA-specific… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3P3I
- Type
- protein
- Length
- 785 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Fluoroacetyl coenzyme a thioesterase
- UniProt
- Q1EMV2
- Ligands
- FAH, COA
- Pockets
- 9 · best druggability 0.83
Structure
x-ray diffraction · 5 distinct chains · 28% helix, 41% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Fluoroacetyl coenzyme a thioesterase | protein | 135 | 28% helix, 40% strand | Q1EMV2 |
| B, F | Fluoroacetyl coenzyme a thioesterase | protein | 133 | 29% helix, 41% strand | Q1EMV2 |
| C | Fluoroacetyl coenzyme a thioesterase | protein | 131 | 29% helix, 41% strand | Q1EMV2 |
| D | Fluoroacetyl coenzyme a thioesterase | protein | 125 | 26% helix, 43% strand | Q1EMV2 |
| E | Fluoroacetyl coenzyme a thioesterase | protein | 128 | 27% helix, 40% strand | Q1EMV2 |
Ligands and binding sites
- FAH · fluoroacetic acid · ligand · 2 copies · chains A, B, C, D
- COA · Coenzyme A · ligand · 2 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
9 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 969 | 0.83 | 0.84 | 104 | FAH, COA |
| 2 | 771 | 0.73 | 0.79 | 81 | empty |
| 3 | 171 | 0.68 | 0.87 | 37 | empty |
| 4 | 298 | 0.66 | 0.82 | 52 | FAH, COA |
| 5 | 176 | 0.65 | 0.85 | 42 | empty |
Interfaces
10 interfaces between chains.
- E–F · 2034 Ų buried · 30 hydrogen bonds · protein-protein
- A–B · 2006 Ų buried · 28 hydrogen bonds · protein-protein
- C–D · 1780 Ų buried · 25 hydrogen bonds · protein-protein
- A–D · 377 Ų buried · 1 hydrogen bond · protein-protein
- B–C · 357 Ų buried · 3 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 3 disulfide (disulfide).
Compared structures
- 3P3I · Crystal structure of the F36A mutant of the fluoroacetyl-CoA-specific thioesterase FlK in… · the same entry in another collection · chain F against F, TM-score 1.00
- Q1EMV2 · AlphaFold monomer V2.0 prediction for fluoroacetyl-CoA thioesterase (Q1EMV2) · a predicted model of the same protein · chain C 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 3P3I · PDBe 3P3I · UniProt Q1EMV2
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