MolNFT v1 · #25547 · protein
Paf-ah holoenzyme: LIS1/ALFA2
1VYH · Platelet-activating factor acetylhydrolase ib beta subunit: “Paf-ah holoenzyme: LIS1/ALFA2”. X-ray diffraction, 20 pockets (best druggability 0.87). MolNFT v1 #25547 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1VYH
- Type
- protein
- Length
- 5,280 residues
- Chains
- 20
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Platelet-activating factor acetylhydrolase ib beta subunit; Platelet-activating factor…
- EC
- 3.1.1.47
- UniProt
- Q29459, P63005
- Pockets
- 20 · best druggability 0.87
Structure
x-ray diffraction · 2 distinct chains · 20% helix, 33% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, E, F, I, J, M, N, Q, R | Platelet-activating factor acetylhydrolase ib beta subunit (EC 3.1.1.47) | protein | 218 | 44% helix, 12% strand | Q29459 |
| C, D, G, H, K, L, O, P, S, T | Platelet-activating factor acetylhydrolase ib alpha subunit | protein | 310 | 2% helix, 48% strand | P63005 |
Pockets
20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 929 | 0.87 | 0.88 | 87 | empty |
| 2 | 930 | 0.86 | 0.88 | 91 | empty |
| 3 | 933 | 0.86 | 0.88 | 90 | empty |
| 4 | 880 | 0.86 | 0.88 | 90 | empty |
| 5 | 1198 | 0.85 | 0.86 | 103 | empty |
Interfaces
32 interfaces between chains.
- Q–R · 1195 Ų buried · 9 hydrogen bonds · protein-protein
- M–N · 1173 Ų buried · 13 hydrogen bonds · protein-protein
- I–J · 1168 Ų buried · 11 hydrogen bonds · protein-protein
- A–B · 1167 Ų buried · 11 hydrogen bonds · protein-protein
- E–F · 1163 Ų buried · 11 hydrogen bonds · protein-protein
Compared structures
- 1VYH · PAF-AH Holoenzyme: Lis1/Alfa2 · the same entry in another collection · chain T against T, 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 Q29459
- Every structure of UniProt P63005
- Elsewhere: RCSB PDB 1VYH · PDBe 1VYH · UniProt Q29459 · UniProt P63005
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