Research workbench
Crystal structure of adenylosuccinate lyase from schistosoma mansoni in complex with AMP
Analyse Crystal structure of adenylosuccinate lyase from schistosoma mansoni in complex… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5EYT
- Type
- protein
- Length
- 472 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Adenylosuccinate lyase
- EC
- 4.3.2.2
- UniProt
- G4VQX9
- Ligands
- AMP
- Pockets
- 3 · best druggability 0.67
Structure
x-ray diffraction · 1 distinct chain · 66% helix, 4% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Adenylosuccinate lyase (EC 4.3.2.2) | protein | 472 | 66% helix, 4% strand | G4VQX9 |
Ligands and binding sites
- AMP · Adenosine monophosphate · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 257 | 0.67 | 0.84 | 33 | empty |
| 2 | 90 | 0.40 | 0.77 | 21 | empty |
| 3 | 79 | 0.37 | 0.77 | 13 | empty |
Compared structures
- 5EYT · Crystal Structure of Adenylosuccinate Lyase from Schistosoma mansoni in complex with AMP · the same entry in another collection · 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 G4VQX9
- Elsewhere: RCSB PDB 5EYT · PDBe 5EYT · UniProt G4VQX9
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