MolNFT v1 · #167279 · protein
Crystal structure of mouse acyl-CoA thioesterase 7 with CoA
6VFY · Cytosolic acyl coenzyme a thioester hydrolase: “Crystal structure of mouse acyl-CoA thioesterase 7 with CoA”. X-ray diffraction, 2 ligands (COA, PO4), 12 pockets (best druggability 0.84). MolNFT v1 #167279 on GenesisL1: 3D…
- PDB
- 6VFY
- Type
- protein
- Length
- 910 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cytosolic acyl coenzyme a thioester hydrolase
- EC
- 3.1.2.2
- UniProt
- Q91V12
- Ligands
- COA, PO4
- Pockets
- 12 · best druggability 0.84
Structure
x-ray diffraction · 2 distinct chains · 26% helix, 36% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| D, E | Cytosolic acyl coenzyme a thioester hydrolase (EC 3.1.2.2) | protein | 303 | 26% helix, 37% strand | Q91V12 |
| F | Cytosolic acyl coenzyme a thioester hydrolase (EC 3.1.2.2) | protein | 304 | 26% helix, 36% strand | Q91V12 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
12 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1194 | 0.84 | 0.85 | 148 | empty |
| 2 | 510 | 0.77 | 0.85 | 55 | COA |
| 3 | 575 | 0.74 | 0.81 | 57 | COA |
| 4 | 345 | 0.69 | 0.82 | 37 | empty |
| 5 | 271 | 0.68 | 0.84 | 37 | empty |
Interfaces
3 interfaces between chains.
- D–E · 1114 Ų buried · 9 hydrogen bonds · protein-protein
- E–F · 983 Ų buried · 8 hydrogen bonds · protein-protein
- D–F · 899 Ų buried · 3 hydrogen bonds · protein-protein
Compared structures
- 6VFY · Crystal structure of mouse acyl-CoA thioesterase 7 with CoA · the same entry in another collection · chain D against D, TM-score 1.00
- Q91V12 · AlphaFold monomer V2.0 prediction for cytosolic acyl coenzyme a thioester hydrolase… · a predicted model of the same protein · chain E against A, TM-score 0.91
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 Q91V12
- Elsewhere: RCSB PDB 6VFY · PDBe 6VFY · UniProt Q91V12
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