Research workbench
Crystal structure of phosphoserine aminotransferase from klebsiella pneumoniae subsp. pneumoniae in complex with pyridoxal phosphate
Analyse Crystal structure of phosphoserine aminotransferase from klebsiella pneumoniae… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7T7J
- Type
- protein
- Length
- 717 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Phosphoserine aminotransferase
- EC
- 2.6.1.52
- UniProt
- A0A0H3GMA6
- Ligands
- PLP
- Pockets
- 9 · best druggability 0.73
Structure
x-ray diffraction · 2 distinct chains · 40% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phosphoserine aminotransferase (EC 2.6.1.52) | protein | 357 | 40% helix, 18% strand | A0A0H3GMA6 |
| B | Phosphoserine aminotransferase (EC 2.6.1.52) | protein | 360 | 40% helix, 19% strand | A0A0H3GMA6 |
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
9 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 448 | 0.73 | 0.83 | 46 | PLP |
| 2 | 490 | 0.71 | 0.81 | 49 | PLP |
| 3 | 56 | 0.52 | 0.87 | 19 | empty |
| 4 | 142 | 0.47 | 0.77 | 26 | empty |
| 5 | 117 | 0.44 | 0.77 | 27 | empty |
Interfaces
1 interface between chains.
- A–B · 2186 Ų buried · 26 hydrogen bonds · protein-protein
Compared structures
- 7T7J · Crystal Structure of Phosphoserine aminotransferase from Klebsiella pneumoniae subsp.… · 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 A0A0H3GMA6
- Elsewhere: RCSB PDB 7T7J · PDBe 7T7J · UniProt A0A0H3GMA6
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