Research workbench
Structure of L-lysine oxidase precursor
Analyse Structure of L-lysine oxidase precursor in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7D4C
- Type
- protein
- Length
- 595 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- L-lysine alpha-oxidase
- UniProt
- A0A0G4DCU0
- Ligands
- FAD, PO4
- Pockets
- 6 · best druggability 0.81
Structure
x-ray diffraction · 1 distinct chain · 36% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | L-lysine alpha-oxidase | protein | 595 | 36% helix, 18% strand | A0A0G4DCU0 |
Ligands and binding sites
- FAD · Flavin-adenine dinucleotide · ligand · chains A
- PO4 · Phosphate ion · ion · 3 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1186 | 0.81 | 0.82 | 109 | FAD |
| 2 | 69 | 0.65 | 0.93 | 25 | empty |
| 3 | 128 | 0.50 | 0.80 | 27 | empty |
| 4 | 115 | 0.43 | 0.77 | 21 | empty |
| 5 | 105 | 0.40 | 0.76 | 24 | empty |
Compared structures
- 7D4C · Structure of L-lysine oxidase precursor · 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 A0A0G4DCU0
- Elsewhere: RCSB PDB 7D4C · PDBe 7D4C · UniProt A0A0G4DCU0
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