Research workbench
E. COLI L-aspartate oxidase: mutant R386L in complex with succinate
Analyse E. COLI L-aspartate oxidase: mutant R386L in complex with succinate in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1KNP
- Type
- protein
- Length
- 529 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- L-aspartate oxidase
- EC
- 1.4.3.16
- UniProt
- P10902
- Ligands
- FAD, NA
- Pockets
- 5 · best druggability 0.83
Structure
x-ray diffraction · 1 distinct chain · 37% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | L-aspartate oxidase (EC 1.4.3.16) | protein | 529 | 37% helix, 18% strand | P10902 |
Ligands and binding sites
- FAD · Flavin-adenine dinucleotide · ligand · chains A
- NA · Sodium ion · metal · chains A
- SIN · Succinic acid · additive · 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, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 437 | 0.83 | 0.90 | 67 | FAD, SIN |
| 2 | 102 | 0.55 | 0.84 | 20 | empty |
| 3 | 164 | 0.49 | 0.77 | 28 | empty |
| 4 | 146 | 0.45 | 0.77 | 23 | empty |
| 5 | 56 | 0.30 | 0.75 | 15 | empty |
Compared structures
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 P10902
- Elsewhere: RCSB PDB 1KNP · PDBe 1KNP · UniProt P10902
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