Research workbench
L201A mutant of D-amino acid aminotransferase complexed with pyridoxal-5'-phosphate
Analyse L201A mutant of D-amino acid aminotransferase complexed with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2DAB
- Type
- protein
- Length
- 562 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- D-amino acid aminotransferase
- EC
- 2.6.1.21
- UniProt
- P19938
- Ligands
- PLP
- Pockets
- 4 · best druggability 0.82
Structure
x-ray diffraction · 2 distinct chains · 29% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | D-amino acid aminotransferase (EC 2.6.1.21) | protein | 280 | 29% helix, 30% strand | P19938 |
| B | D-amino acid aminotransferase (EC 2.6.1.21) | protein | 282 | 29% helix, 30% strand | P19938 |
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
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 877 | 0.82 | 0.85 | 113 | PLP |
| 2 | 65 | 0.37 | 0.78 | 13 | empty |
| 3 | 51 | 0.36 | 0.79 | 11 | empty |
| 4 | 54 | 0.28 | 0.74 | 16 | empty |
Interfaces
1 interface between chains.
- A–B · 2394 Ų buried · 25 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 cofactor (pyridoxal phosphate Schiff base).
Compared structures
- 2DAB · L201A mutant of D-amino acid aminotransferase complexed with pyridoxal-5'-phosphate · the same entry in another collection · chain A against A, TM-score 1.00
- P19938 · AlphaFold monomer V2.0 prediction for D-alanine aminotransferase (P19938) · 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 P19938
- Elsewhere: RCSB PDB 2DAB · PDBe 2DAB · UniProt P19938
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