MolNFT v1 · #101987 · protein
Saicar synthetase (type-2) in complex with ADP and cdp
4O86 · Phosphoribosylaminoimidazole-succinocarboxamide synthase: “Saicar synthetase (type-2) in complex with ADP and cdp”. X-ray diffraction, 5 ligands (CDP, C5P, ADP), 1 pocket (best druggability 0.64). MolNFT v1 #101987 on GenesisL1: 3D…
- PDB
- 4O86
- Type
- protein
- Length
- 227 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
- O57978
- Ligands
- CDP, C5P, ADP, MG, PO4
- Pockets
- 1 · best druggability 0.64
Structure
x-ray diffraction · 1 distinct chain · 32% helix, 32% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phosphoribosylaminoimidazole-succinocarboxamide synthase (EC 6.3.2.6) | protein | 227 | 32% helix, 32% strand | O57978 |
Ligands and binding sites
- CDP · Cytidine-5'-diphosphate · ligand · chains A
- C5P · Cytidine-5'-monophosphate · ligand · chains A
- ADP · Adenosine-5'-diphosphate · ligand · chains A
- MG · Magnesium ion · metal · chains A
- PO4 · Phosphate ion · ion · 2 copies · chains A
- ACT · Acetate ion · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 479 | 0.64 | 0.77 | 44 | PO4, CDP, C5P, MG, ADP |
Compared structures
- 4O86 · SAICAR synthetase (Type-2) in complex with ADP and CDP · the same entry in another collection · chain A against A, TM-score 1.00
- O57978 · AlphaFold monomer V2.0 prediction for phosphoribosylaminoimidazole- succinocarboxamide… · a predicted model of the same protein · chain A against A, TM-score 0.99
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 O57978
- Elsewhere: RCSB PDB 4O86 · PDBe 4O86 · UniProt O57978
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