Research workbench
Crystal structure of the human acyl protein thioesterase 1 at 1.5 a resolution
Analyse Crystal structure of the human acyl protein thioesterase 1 at 1.5 a resolution in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1FJ2
- Type
- protein
- Length
- 458 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein (acyl protein thioesterase 1)
- EC
- 3.1.4.39
- UniProt
- O75608
- Ligands
- BR
- Pockets
- 4 · best druggability 0.84
Structure
x-ray diffraction · 1 distinct chain · 37% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Protein (acyl protein thioesterase 1) (EC 3.1.4.39) | protein | 229 | 37% helix, 21% strand | O75608 |
Ligands and binding sites
- BR · Bromide ion · ion · 40 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 311 | 0.84 | 0.94 | 47 | BR |
| 2 | 95 | 0.60 | 0.87 | 22 | empty |
| 3 | 110 | 0.57 | 0.84 | 16 | BR |
| 4 | 62 | 0.55 | 0.88 | 16 | BR |
Interfaces
1 interface between chains.
- A–B · 1228 Ų buried · 5 hydrogen bonds · protein-protein
Compared structures
- 1FJ2 · Crystal structure of the human acyl protein thioesterase 1 at 1.5 A resolution · the same entry in another collection · chain A against A, TM-score 1.00
- O75608 · AlphaFold monomer V2.0 prediction for acyl-protein thioesterase 1 (O75608) · a predicted model of the same protein · chain A against A, TM-score 0.97
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 O75608
- Elsewhere: RCSB PDB 1FJ2 · PDBe 1FJ2 · UniProt O75608
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