GL1X · GenesisL1 explorer

Research workbench

PFS25 in complex with the human transmission blocking antibody 2586

Analyse PFS25 in complex with the human transmission blocking antibody 2586 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6PHD
Type
protein
Length
600 residues
Chains
3
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
2586 antibody Fab, heavy chain; 2586 antibody Fab, light chain; 25 kda ookinete surface…
UniProt
P13829
Pockets
7 · best druggability 0.61

Structure

x-ray diffraction · 3 distinct chains · 7% helix, 50% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
H2586 antibody Fab, heavy chainprotein2248% helix, 53% strand—
L2586 antibody Fab, light chainprotein2098% helix, 49% strand—
C25 kda ookinete surface antigenprotein1674% helix, 46% strandP13829

Pockets

7 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13770.610.7746empty
25530.610.7456empty
31280.400.7425empty
41060.370.7416empty
5930.350.7418empty

Interfaces

3 interfaces between chains.

  • H–L · 1693 Ų buried · 12 hydrogen bonds · protein-protein
  • H–C · 489 Ų buried · 11 hydrogen bonds · protein-protein
  • L–C · 459 Ų buried · 9 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 15 disulfide (disulfide).

Compared structures

  • 6PHD · Pfs25 in complex with the human transmission blocking antibody 2586 · the same entry in another collection · chain H against H, TM-score 1.00
  • P13829 · AlphaFold monomer V2.0 prediction for 25 kda ookinete surface antigen (P13829) · a predicted model of the same protein · chain C against A, TM-score 0.98

Analyse

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.