Research workbench
Crystal structure of aryl-alcohol oxidase from pleurotus eryngii in complex with P-anisic acid
Analyse Crystal structure of aryl-alcohol oxidase from pleurotus eryngii in complex… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5OC1
- Type
- protein
- Length
- 565 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- O94219
- Ligands
- ANN, FAD
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 565 | — | O94219 |
Ligands and binding sites
- ANN · 4-methoxybenzoic acid · ligand · chains A
- FAD · Flavin-adenine dinucleotide · ligand · chains A
- GOL · Glycerol · additive · 5 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 5OC1 · Crystal structure of aryl-alcohol oxidase from Pleurotus eryngii in complex with p-anisic… · 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 O94219
- Elsewhere: RCSB PDB 5OC1 · PDBe 5OC1 · UniProt O94219
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.