Research workbench
Crystal structure of 45 amino acid deleted from N-terminal of phosphoserine aminotransferase (psat) of entamoeba histolytica
Analyse Crystal structure of 45 amino acid deleted from N-terminal of phosphoserine… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5YII
- Type
- protein
- Length
- 311 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Phosphoserine aminotransferase
- EC
- 2.6.1.52
- UniProt
- Q60I38
- Ligands
- SCN
- Pockets
- 4 · best druggability 0.65
Structure
x-ray diffraction · 1 distinct chain · 43% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phosphoserine aminotransferase (EC 2.6.1.52) | protein | 311 | 43% helix, 18% strand | Q60I38 |
Ligands and binding sites
- SCN · Thiocyanate ion · ion · chains A
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 | 367 | 0.65 | 0.80 | 41 | empty |
| 2 | 106 | 0.53 | 0.83 | 26 | SCN |
| 3 | 60 | 0.37 | 0.78 | 14 | empty |
| 4 | 55 | 0.28 | 0.74 | 11 | empty |
Compared structures
- 5YII · Crystal Structure of 45 amino acid deleted from N-terminal of Phosphoserine… · 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 5YII · PDBe 5YII · UniProt Q60I38
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.