Research workbench
Structure of L-lysine oxidase precursor in complex with L-lysine (1.24M)
Analyse Structure of L-lysine oxidase precursor in complex with L-lysine (1.24M) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7D4D
- Type
- protein
- Length
- 506 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- L-lysine alpha-oxidase
- UniProt
- A0A0G4DCU0
- Ligands
- FAD, LYS
- Pockets
- 4 · best druggability 0.85
Structure
x-ray diffraction · 1 distinct chain · 40% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | L-lysine alpha-oxidase | protein | 506 | 40% helix, 20% strand | A0A0G4DCU0 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 360 | 0.85 | 0.94 | 65 | FAD, LYS |
| 2 | 579 | 0.74 | 0.81 | 51 | empty |
| 3 | 167 | 0.44 | 0.74 | 30 | empty |
| 4 | 65 | 0.28 | 0.73 | 18 | empty |
Compared structures
- 7D4D · Structure of L-lysine oxidase precursor in complex with L-lysine (1.24M) · 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 7D4D · PDBe 7D4D · UniProt A0A0G4DCU0
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