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The structure of a glutathione synthetase (STGSS1) from solanum tuberosum in ADP and Y-ec bound closed conformation.
Analyse The structure of a glutathione synthetase (STGSS1) from solanum tuberosum in… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5OES
- Type
- protein
- Length
- 2,680 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- M1CSC4
- Ligands
- ADP, 3GC, MG
Structure
x-ray diffraction · 6 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 445 | — | M1CSC4 |
| B | — | protein | 446 | — | M1CSC4 |
| C | — | protein | 447 | — | M1CSC4 |
| D | — | protein | 446 | — | M1CSC4 |
| E | — | protein | 448 | — | M1CSC4 |
| F | — | protein | 448 | — | M1CSC4 |
Ligands and binding sites
- ADP · Adenosine-5'-diphosphate · ligand · 6 copies · chains A, B, C, D, E, F
- 3GC · Gamma-glutamylcysteine · ligand · 6 copies · chains A, B, C, D, E, F
- MG · Magnesium ion · metal · 10 copies · chains A, B, C, D, E, F
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
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 M1CSC4
- Elsewhere: RCSB PDB 5OES · PDBe 5OES · UniProt M1CSC4
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