Research workbench
Structure of L-glutamate oxidase R305E mutant
Analyse Structure of L-glutamate oxidase R305E mutant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7E0C
- Type
- protein
- Length
- 591 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- L-glutamate oxidase
- EC
- 1.4.3.11
- UniProt
- Q8L3C7
- Ligands
- FAD
- Pockets
- 5 · best druggability 0.88
Structure
x-ray diffraction · 1 distinct chain · 36% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | L-glutamate oxidase (EC 1.4.3.11) | protein | 591 | 36% helix, 22% strand | Q8L3C7 |
Ligands and binding sites
- FAD · Flavin-adenine dinucleotide · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1142 | 0.88 | 0.89 | 137 | FAD |
| 2 | 151 | 0.81 | 0.97 | 28 | empty |
| 3 | 158 | 0.52 | 0.79 | 30 | empty |
| 4 | 222 | 0.46 | 0.73 | 31 | empty |
| 5 | 61 | 0.40 | 0.80 | 10 | empty |
Compared structures
- 7E0C · Structure of L-glutamate oxidase R305E mutant · 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 Q8L3C7
- Elsewhere: RCSB PDB 7E0C · PDBe 7E0C · UniProt Q8L3C7
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