Research workbench
Neutron structure of copper amine oxidase from Arthrobacter glibiformis at pD 7.4
Analyse Neutron structure of copper amine oxidase from Arthrobacter glibiformis at pD… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6L9C
- Type
- protein
- Length
- 621 residues
- Chains
- 1
- Method
- x-ray diffraction, neutron diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.14,1.72
- Source
- Arthrobacter globiformis
- Molecule
- Phenylethylamine oxidase
- EC
- 1.4.3.21
- UniProt
- P46881
- Ligands
- CU, NA
- Pockets
- 7 · best druggability 0.67
Structure
x-ray diffraction, neutron diffraction · resolution 1.14,1.72 · 1 distinct chain · 13% helix, 42% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| X | Phenylethylamine oxidase (EC 1.4.3.21) | protein | 621 | 13% helix, 42% strand | P46881 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 57 | 0.67 | 0.96 | 27 | empty |
| 2 | 241 | 0.61 | 0.81 | 48 | empty |
| 3 | 63 | 0.47 | 0.84 | 16 | empty |
| 4 | 177 | 0.46 | 0.75 | 31 | empty |
| 5 | 171 | 0.45 | 0.75 | 37 | empty |
Modifications
Observed in the structure: 2 modified, 1 disulfide (nonstandard, disulfide).
Compared structures
- 6L9C · Neutron structure of copper amine oxidase from arthrobacter glibiformis at pd 7.4 · the same entry in another collection · chain X against X, TM-score 1.00
- P46881 · AlphaFold monomer V2.0 prediction for phenylethylamine oxidase (P46881) · a predicted model of the same protein · chain X 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 6L9C · PDBe 6L9C · UniProt P46881
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