Research workbench
Crystal structure of phosphoserine aminotransferase from bacillus circulans var. alkalophilus at pH 8.5
Analyse Crystal structure of phosphoserine aminotransferase from bacillus circulans… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2C0R
- Type
- protein
- Length
- 722 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Phosphoserine aminotransferase
- EC
- 2.6.1.52
- UniProt
- Q59196
- Ligands
- PLP
- Pockets
- 8 · best druggability 0.74
Structure
x-ray diffraction · 1 distinct chain · 41% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Phosphoserine aminotransferase (EC 2.6.1.52) | protein | 361 | 41% helix, 17% strand | Q59196 |
Ligands and binding sites
- PLP · Pyridoxal-5'-phosphate · ligand · 2 copies · 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, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 70 | 0.74 | 0.98 | 28 | empty |
| 2 | 357 | 0.67 | 0.81 | 50 | PLP |
| 3 | 363 | 0.64 | 0.79 | 55 | PLP |
| 4 | 78 | 0.43 | 0.80 | 25 | empty |
| 5 | 68 | 0.40 | 0.80 | 14 | empty |
Interfaces
1 interface between chains.
- A–B · 2349 Ų buried · 35 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 cofactor (pyridoxal phosphate Schiff base).
Compared structures
- 2C0R · CRYSTAL STRUCTURE OF PHOSPHOSERINE AMINOTRANSFERASE FROM BACILLUS CIRCULANS VAR.… · the same entry in another collection · chain A against A, TM-score 1.00
- Q59196 · AlphaFold monomer V2.0 prediction for phosphoserine aminotransferase (Q59196) · a predicted model of the same protein · 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 Q59196
- Elsewhere: RCSB PDB 2C0R · PDBe 2C0R · UniProt Q59196
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