Research workbench
Crystal structure of human plasma platelet activating factor acetylhydrolase covalently inhibited by sarin
Analyse Crystal structure of human plasma platelet activating factor acetylhydrolase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3F96
- Type
- protein
- Length
- 742 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Platelet-activating factor acetylhydrolase
- EC
- 3.1.1.47
- UniProt
- Q13093
- Pockets
- 8 · best druggability 0.59
Structure
x-ray diffraction · 1 distinct chain · 38% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Platelet-activating factor acetylhydrolase (EC 3.1.1.47) | protein | 371 | 38% helix, 20% strand | Q13093 |
Pockets
8 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 162 | 0.59 | 0.82 | 24 | empty |
| 2 | 167 | 0.56 | 0.80 | 23 | empty |
| 3 | 251 | 0.50 | 0.75 | 32 | empty |
| 4 | 83 | 0.41 | 0.79 | 15 | empty |
| 5 | 75 | 0.37 | 0.77 | 18 | empty |
Interfaces
1 interface between chains.
- A–B · 692 Ų buried · 8 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 modified (nonstandard).
Compared structures
- 3F96 · Crystal structure of human plasma platelet activating factor acetylhydrolase covalently… · the same entry in another collection · chain A against A, TM-score 1.00
- Q13093 · AlphaFold monomer V2.0 prediction for platelet-activating factor acetylhydrolase (Q13093) · a predicted model of the same protein · chain A against A, TM-score 1.00
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 Q13093
- Elsewhere: RCSB PDB 3F96 · PDBe 3F96 · UniProt Q13093
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