MolNFT v1 · #47246 · protein
Probable glutaminase from bacillus subtilis complexed with 6-diazo-5-oxo-L-norleucine
2OSU · Glutaminase 1: “Probable glutaminase from bacillus subtilis complexed with 6-diazo-5-oxo-L-norleucine”. X-ray diffraction, 1 ligand (DON), 7 pockets (best druggability 0.64). MolNFT v1 #47246 on GenesisL1: 3D structure, binding…
- PDB
- 2OSU
- Type
- protein
- Length
- 609 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glutaminase 1
- EC
- 3.5.1.2
- UniProt
- O31465
- Ligands
- DON
- Pockets
- 7 · best druggability 0.64
Structure
x-ray diffraction · 2 distinct chains · 49% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glutaminase 1 (EC 3.5.1.2) | protein | 306 | 49% helix, 13% strand | O31465 |
| B | Glutaminase 1 (EC 3.5.1.2) | protein | 303 | 50% helix, 13% strand | O31465 |
Ligands and binding sites
- DON · 6-diazenyl-5-oxo-L-norleucine · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 424 | 0.64 | 0.78 | 59 | empty |
| 2 | 212 | 0.53 | 0.78 | 39 | DON |
| 3 | 107 | 0.53 | 0.82 | 20 | DON |
| 4 | 144 | 0.43 | 0.75 | 17 | empty |
| 5 | 118 | 0.42 | 0.76 | 17 | empty |
Interfaces
1 interface between chains.
- A–B · 1120 Ų buried · 14 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 24 modified (engineered).
Compared structures
- 2OSU · Probable glutaminase from Bacillus subtilis complexed with 6-diazo-5-oxo-L-norleucine · the same entry in another collection · chain A against A, TM-score 1.00
- O31465 · AlphaFold monomer V2.0 prediction for glutaminase 1 (O31465) · a predicted model of the same protein · chain B 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 O31465
- Elsewhere: RCSB PDB 2OSU · PDBe 2OSU · UniProt O31465
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