MolNFT v1 · #153877 · protein
Crystal structure of 450-451_DELETION mutant of fgam synthetase
6JT8 · Phosphoribosylformylglycinamidine synthase: “Crystal structure of 450-451_DELETION mutant of fgam synthetase”. X-ray diffraction, 3 ligands (ADP, MG, SO4), 10 pockets (best druggability 0.85). MolNFT v1 #153877 on GenesisL1: 3D…
- PDB
- 6JT8
- Type
- protein
- Length
- 1,288 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Phosphoribosylformylglycinamidine synthase
- EC
- 6.3.5.3
- UniProt
- A0A0D6F9Y3
- Ligands
- ADP, MG, SO4
- Pockets
- 10 · best druggability 0.85
Structure
x-ray diffraction · 1 distinct chain · 35% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phosphoribosylformylglycinamidine synthase (EC 6.3.5.3) | protein | 1288 | 35% helix, 27% strand | A0A0D6F9Y3 |
Ligands and binding sites
- ADP · Adenosine-5'-diphosphate · ligand · chains A
- MG · Magnesium ion · metal · 3 copies · chains A
- SO4 · Sulfate ion · ion · 17 copies · chains A
- GOL · Glycerol · additive · 18 copies · chains A
- EDO · 1,2-ethanediol · additive · 11 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
10 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 285 | 0.85 | 0.97 | 49 | ADP, MG |
| 2 | 1005 | 0.83 | 0.84 | 95 | SO4, GOL |
| 3 | 268 | 0.79 | 0.91 | 39 | GOL |
| 4 | 119 | 0.78 | 0.97 | 32 | EDO |
| 5 | 1001 | 0.78 | 0.80 | 81 | EDO, SO4 |
Modifications
Observed in the structure: 1 modified (nonstandard).
Compared structures
- 6JT8 · Crystal structure of 450-451_deletion mutant of FGAM Synthetase · 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 A0A0D6F9Y3
- Elsewhere: RCSB PDB 6JT8 · PDBe 6JT8 · UniProt A0A0D6F9Y3
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