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Crystallographic structure of copper amine oxidase from arthrobacter glibiformis at pd 7.4 determined by only neutron diffraction data.

Analyse Crystallographic structure of copper 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
7WNO
Type
protein
Length
621 residues
Chains
1
Method
neutron diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Phenylethylamine oxidase
EC
1.4.3.21
UniProt
P46881
Ligands
CU
Pockets
6 · best druggability 0.61

Structure

neutron diffraction · 1 distinct chain · 13% helix, 42% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
XPhenylethylamine oxidase (EC 1.4.3.21)protein62113% helix, 42% strandP46881

Ligands and binding sites

  • CU · Copper (II) ion · metal · chains X

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

6 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12800.610.8052empty
22270.600.8026empty
3740.450.8217empty
41350.430.7530empty
5700.360.7718empty

Modifications

Observed in the structure: 2 modified, 1 disulfide (nonstandard, disulfide).

Compared structures

  • 7WNO · Crystallographic structure of copper amine oxidase from Arthrobacter glibiformis at pD… · the same entry in another collection · chain X against X, TM-score 1.00

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