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Structure of the glutaminase subunit PDX2 (yaae) of plp synthase from bacillus subtilis
Analyse Structure of the glutaminase subunit PDX2 (yaae) of plp synthase from bacillus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2NV0
- Type
- protein
- Length
- 378 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glutamine amidotransferase subunit pdxt
- EC
- 2.6.-.-
- UniProt
- P37528
- Pockets
- 5 · best druggability 0.59
Structure
x-ray diffraction · 2 distinct chains · 30% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glutamine amidotransferase subunit pdxt (EC 2.6.-.-) | protein | 191 | 29% helix, 30% strand | P37528 |
| B | Glutamine amidotransferase subunit pdxt (EC 2.6.-.-) | protein | 187 | 30% helix, 30% strand | P37528 |
Pockets
5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 322 | 0.59 | 0.77 | 35 | empty |
| 2 | 162 | 0.53 | 0.79 | 27 | empty |
| 3 | 68 | 0.47 | 0.83 | 17 | empty |
| 4 | 50 | 0.36 | 0.80 | 13 | empty |
| 5 | 107 | 0.36 | 0.73 | 16 | empty |
Interfaces
1 interface between chains.
- A–B · 449 Ų buried · 4 hydrogen bonds · protein-protein
Compared structures
- 2NV0 · Structure of the glutaminase subunit Pdx2 (YaaE) of PLP synthase from Bacillus subtilis · the same entry in another collection · chain A against A, TM-score 1.00
- P37528 · AlphaFold monomer V2.0 prediction for pyridoxal 5'-phosphate synthase subunit pdxt… · a predicted model of the same protein · chain A against A, TM-score 0.97
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 P37528
- Elsewhere: RCSB PDB 2NV0 · PDBe 2NV0 · UniProt P37528
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