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Atomic resolution structure of saicar-synthase from saccharomyces cerevisiae complexed with aspartic acid
Analyse Atomic resolution structure of saicar-synthase from saccharomyces cerevisiae… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2CNU
- Type
- protein
- Length
- 302 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Phosphoribosylaminoimidazole-succinocarboxamide synthase
- EC
- 6.3.2.6
- UniProt
- P27616
- Ligands
- ASP, ACE, SO4
- Pockets
- 2 · best druggability 0.71
Structure
x-ray diffraction · 1 distinct chain · 33% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phosphoribosylaminoimidazole-succinocarboxamide synthase (EC 6.3.2.6) | protein | 302 | 33% helix, 23% strand | P27616 |
Ligands and binding sites
- ASP · Aspartic acid · ligand · 3 copies · chains A
- ACE · Acetyl group · ligand · chains A
- SO4 · Sulfate ion · ion · 7 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 773 | 0.71 | 0.77 | 75 | ASP, SO4 |
| 2 | 82 | 0.35 | 0.75 | 16 | empty |
Modifications
Observed in the structure: 1 covalent (covalent ligand).
Compared structures
- 2CNU · Atomic resolution structure of SAICAR-synthase from Saccharomyces cerevisiae complexed… · the same entry in another collection · chain A against A, TM-score 1.00
- P27616 · AlphaFold monomer V2.0 prediction for phosphoribosylaminoimidazole- succinocarboxamide… · a predicted model of the same protein · chain A against A, TM-score 0.96
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 P27616
- Elsewhere: RCSB PDB 2CNU · PDBe 2CNU · UniProt P27616
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