MolNFT v1 · #46124 · protein
Structure of the glutaminase subunit PDX2 (yaae) of plp synthase from bacillus subtilis
2NV0 · Glutamine amidotransferase subunit pdxt: “Structure of the glutaminase subunit PDX2 (yaae) of plp synthase from bacillus subtilis”. X-ray diffraction, 5 pockets (best druggability 0.59). MolNFT v1 #46124 on GenesisL1: 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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