Research workbench
The structure of phosphoserine aminotransferase from E. COLI in complex with alpha-methyl-L-glutamate
Analyse The structure of phosphoserine aminotransferase from E. COLI in complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1BJO
- Type
- protein
- Length
- 720 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Phosphoserine aminotransferase
- EC
- 2.6.1.52
- Ligands
- PLP, GAM
- Pockets
- 8 · best druggability 0.72
Structure
x-ray diffraction · 1 distinct chain · 39% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Phosphoserine aminotransferase (EC 2.6.1.52) | protein | 360 | 39% helix, 19% strand | — |
Ligands and binding sites
- PLP · Pyridoxal-5'-phosphate · ligand · chains A, B
- GAM · Alpha-methyl-L-glutamic acid · ligand · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 474 | 0.72 | 0.81 | 52 | PLP, GAM |
| 2 | 413 | 0.68 | 0.80 | 37 | empty |
| 3 | 122 | 0.44 | 0.77 | 26 | empty |
| 4 | 116 | 0.43 | 0.77 | 21 | empty |
| 5 | 56 | 0.34 | 0.78 | 14 | empty |
Interfaces
1 interface between chains.
- A–B · 2303 Ų buried · 30 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 modified (cofactor).
Compared structures
- 1BJO · The structure of phosphoserine aminotransferase from E. COLI in complex with… · 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
- Elsewhere: RCSB PDB 1BJO · PDBe 1BJO
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