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Paf-ah holoenzyme: LIS1/ALFA2

Analyse Paf-ah holoenzyme: LIS1/ALFA2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

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).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, E, F, I, J, M, N, Q, RPlatelet-activating factor acetylhydrolase ib beta subunit (EC 3.1.1.47)protein21844% helix, 12% strandQ29459
C, D, G, H, K, L, O, P, S, TPlatelet-activating factor acetylhydrolase ib alpha subunitprotein3102% helix, 48% strandP63005

Pockets

20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
19290.870.8887empty
29300.860.8891empty
39330.860.8890empty
48800.860.8890empty
511980.850.86103empty

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

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