Research workbench
Crystal structure of the fluoroacetyl-CoA-specific thioesterase flk in complex with fluoroacetate
Analyse Crystal structure of the fluoroacetyl-CoA-specific thioesterase flk in complex… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3P2R
- Type
- protein
- Length
- 266 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Fluoroacetyl coenzyme a thioesterase
- UniProt
- Q1EMV2
- Ligands
- FAH
- Pockets
- 3 · best druggability 0.64
Structure
x-ray diffraction · 1 distinct chain · 29% helix, 40% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Fluoroacetyl coenzyme a thioesterase | protein | 133 | 29% helix, 40% strand | Q1EMV2 |
Ligands and binding sites
- FAH · fluoroacetic acid · ligand · 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 | 211 | 0.64 | 0.83 | 41 | FAH |
| 2 | 151 | 0.61 | 0.84 | 36 | FAH |
| 3 | 64 | 0.41 | 0.80 | 13 | empty |
Interfaces
1 interface between chains.
- A–B · 2026 Ų buried · 29 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 3P2R · Crystal structure of the fluoroacetyl-CoA-specific thioesterase FlK in complex with… · 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 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 3P2R · PDBe 3P2R · UniProt Q1EMV2
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