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Crystal structure of faicar synthetase (purp) from M. jannaschii complexed with ATP and aicar
Analyse Crystal structure of faicar synthetase (purp) from M. jannaschii complexed with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2R7L
- Type
- protein
- Length
- 355 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 5-formaminoimidazole-4-carboxamide-1-(beta)-D-ribofuranosyl 5'-monophosphate synthetase
- EC
- 6.3.4.-
- UniProt
- Q57600
- Ligands
- ATP, AMZ, CL, SO4
- Pockets
- 1 · best druggability 0.66
Structure
x-ray diffraction · 1 distinct chain · 41% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 5-formaminoimidazole-4-carboxamide-1-(beta)-D-ribofuranosyl 5'-monophosphate synthetase (EC 6.3.4.-) | protein | 355 | 41% helix, 23% strand | Q57600 |
Ligands and binding sites
- ATP · Adenosine-5'-triphosphate · ligand · chains A
- AMZ · Aminoimidazole 4-carboxamide ribonucleotide · ligand · chains A
- CL · Chloride ion · ion · 2 copies · chains A
- SO4 · Sulfate ion · ion · 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 | 472 | 0.66 | 0.78 | 46 | CL, ATP, AMZ |
Compared structures
- 2R7L · Crystal structure of FAICAR synthetase (PurP) from M. jannaschii complexed with ATP and… · the same entry in another collection · chain A against A, TM-score 1.00
- Q57600 · AlphaFold monomer V2.0 prediction for 5-formaminoimidazole-4-carboxamide-1-(beta)-D-ribofu… · a predicted model of the same protein · chain A against A, TM-score 0.98
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 Q57600
- Elsewhere: RCSB PDB 2R7L · PDBe 2R7L · UniProt Q57600
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