Research workbench
Crystal structure of wild type phosphoserine aminotransferase (psat) from E. histolytica
Analyse Crystal structure of wild type phosphoserine aminotransferase (psat) from E.… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5YB0
- Type
- protein
- Length
- 3,866 residues
- Chains
- 12
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q60I38
- Ligands
- PLP, CL
Structure
x-ray diffraction · 10 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 348 | — | Q60I38 |
| B, C, H | — | protein | 349 | — | Q60I38 |
| D | — | protein | 345 | — | Q60I38 |
| E | — | protein | 342 | — | Q60I38 |
| F | — | protein | 322 | — | Q60I38 |
| G | — | protein | 341 | — | Q60I38 |
| I | — | protein | 336 | — | Q60I38 |
| J | — | protein | 253 | — | Q60I38 |
| K | — | protein | 316 | — | Q60I38 |
| L | — | protein | 216 | — | Q60I38 |
Ligands and binding sites
- PLP · Pyridoxal-5'-phosphate · ligand · 10 copies · chains A, B, C, D, E, H, F, G, I, J, K, L
- CL · Chloride ion · ion · 5 copies · chains A, B, C, D, E
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 5YB0 · Crystal Structure of Wild Type Phosphoserine aminotransferase (PSAT) from E. histolytica · 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 Q60I38
- Elsewhere: RCSB PDB 5YB0 · PDBe 5YB0 · UniProt Q60I38
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