Research workbench
Structural basis of the activity and substrate specificity of the fluoroacetyl-CoA thioesterase flk
Analyse Structural basis of the activity and substrate specificity of the… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3KX8
- Type
- protein
- Length
- 1,066 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q1EMV2
Structure
x-ray diffraction · 4 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, D, E, F, G | — | protein | 133 | — | Q1EMV2 |
| B | — | protein | 135 | — | Q1EMV2 |
| C | — | protein | 132 | — | Q1EMV2 |
| H | — | protein | 134 | — | Q1EMV2 |
Compared structures
- 3KX8 · 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 3KX8 · PDBe 3KX8 · UniProt Q1EMV2
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