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Crystal structure of adenylosuccinate lyase from schistosoma mansoni in apo form.

Analyse Crystal structure of adenylosuccinate lyase from schistosoma mansoni in apo… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5EYV
Type
protein
Length
886 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Adenylosuccinate lyase
EC
4.3.2.2
UniProt
G4VQX9
Pockets
13 · best druggability 0.80

Structure

x-ray diffraction · 2 distinct chains · 68% helix, 4% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AAdenylosuccinate lyase (EC 4.3.2.2)protein46668% helix, 4% strandG4VQX9
BAdenylosuccinate lyase (EC 4.3.2.2)protein42068% helix, 4% strandG4VQX9

Pockets

13 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11470.800.9625empty
2750.760.9920empty
3740.760.9920empty
46340.700.7865empty
52490.650.8233empty

Interfaces

1 interface between chains.

  • A–B · 3543 Ų buried · 62 hydrogen bonds · protein-protein

Compared structures

  • 5EYV · Crystal Structure of Adenylosuccinate lyase from Schistosoma mansoni in APO form. · the same entry in another collection · chain A against A, TM-score 1.00

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