Research workbench
Saicar synthetase (type-2) in complex with ADP, asp and tmp
Analyse Saicar synthetase (type-2) in complex with ADP, asp and tmp in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4O7T
- Type
- protein
- Length
- 225 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
- TMP, ADP, ASP
- Pockets
- 1 · best druggability 0.64
Structure
x-ray diffraction · 1 distinct chain · 31% helix, 32% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phosphoribosylaminoimidazole-succinocarboxamide synthase (EC 6.3.2.6) | protein | 225 | 31% helix, 32% strand | O57978 |
Ligands and binding sites
- TMP · Thymidine-5'-phosphate · ligand · chains A
- ADP · Adenosine-5'-diphosphate · ligand · chains A
- ASP · Aspartic acid · ligand · chains A
- ACT · Acetate ion · additive · 2 copies · 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 | 461 | 0.64 | 0.77 | 34 | TMP, ASP, ACT |
Compared structures
- 4O7T · SAICAR synthetase (Type-2) in complex with ADP, ASP and TMP · 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 4O7T · PDBe 4O7T · UniProt O57978
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