Research workbench
Saicar synthetase complexed with ADP-MG2+
Analyse Saicar synthetase complexed with ADP-MG2+ in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2GQR
- Type
- protein
- Length
- 474 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Phosphoribosylaminoimidazole-succinocarboxamide synthase
- EC
- 6.3.2.6
- UniProt
- P0A7D7
- Ligands
- ADP, MG
- Pockets
- 4 · best druggability 0.76
Structure
x-ray diffraction · 1 distinct chain · 31% helix, 32% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Phosphoribosylaminoimidazole-succinocarboxamide synthase (EC 6.3.2.6) | protein | 237 | 31% helix, 32% strand | P0A7D7 |
Ligands and binding sites
- ADP · Adenosine-5'-diphosphate · ligand · 2 copies · chains A, B
- MG · Magnesium ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 627 | 0.76 | 0.82 | 59 | MG, ADP |
| 2 | 590 | 0.75 | 0.82 | 55 | MG, ADP |
| 3 | 184 | 0.50 | 0.77 | 37 | empty |
| 4 | 51 | 0.27 | 0.74 | 12 | empty |
Interfaces
1 interface between chains.
- A–B · 996 Ų buried · 16 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 18 modified (engineered).
Compared structures
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 P0A7D7
- Elsewhere: RCSB PDB 2GQR · PDBe 2GQR · UniProt P0A7D7
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