MolNFT v2 · #156524 · protein
Neutron structure of copper amine oxidase from Arthrobacter glibiformis at pD 7.4
6L9C · Phenylethylamine oxidase: “Neutron structure of copper amine oxidase from Arthrobacter glibiformis at pD 7.4”. X-ray diffraction, neutron diffraction at 1.14,1.72, 2 ligands (CU, NA), 7 pockets (best druggability 0.67). MolNFT v2…
- 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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