Research workbench
Crystal structures of the copper-containing amine oxidase from arthrobacter globiformis in the holo-and apo-forms: implications for the biogenesis of topa quinone
Analyse Crystal structures of the copper-containing amine oxidase from arthrobacter… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1AV4
- Type
- protein
- Length
- 620 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Amine oxidase
- EC
- 1.4.3.6
- UniProt
- P46881
- Ligands
- CU
- Pockets
- 6 · best druggability 0.61
Structure
x-ray diffraction · 1 distinct chain · 13% helix, 42% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Amine oxidase (EC 1.4.3.6) | protein | 620 | 13% helix, 42% strand | P46881 |
Ligands and binding sites
- CU · Copper (II) ion · metal · 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, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 190 | 0.61 | 0.83 | 34 | empty |
| 2 | 181 | 0.50 | 0.76 | 22 | empty |
| 3 | 63 | 0.38 | 0.80 | 16 | empty |
| 4 | 93 | 0.37 | 0.75 | 22 | empty |
| 5 | 74 | 0.34 | 0.76 | 18 | empty |
Modifications
Observed in the structure: 1 disulfide, 1 modified (disulfide, nonstandard).
Compared structures
- 1AV4 · Crystal structures of the copper-containing amine oxidase from arthrobacter globiformis… · the same entry in another collection · chain A against A, TM-score 1.00
- P46881 · AlphaFold monomer V2.0 prediction for phenylethylamine oxidase (P46881) · a predicted model of the same protein · 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 P46881
- Elsewhere: RCSB PDB 1AV4 · PDBe 1AV4 · UniProt P46881
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