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Copper amine oxidase from arthrobacter globiformis anaerobically reduced by ethylamine at pH 7 at 288 K (2)

Analyse Copper amine oxidase from arthrobacter globiformis anaerobically reduced by… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5ZOY
Type
protein
Length
1,240 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Phenylethylamine oxidase
EC
1.4.3.21
UniProt
P46881
Ligands
NA, CU
Pockets
12 · best druggability 0.77

Structure

x-ray diffraction · 1 distinct chain · 13% helix, 42% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BPhenylethylamine oxidase (EC 1.4.3.21)protein62013% helix, 42% strandP46881

Ligands and binding sites

  • NA · Sodium ion · metal · 3 copies · chains A, B
  • CU · Copper (II) ion · metal · 2 copies · chains A, B
  • EDO · 1,2-ethanediol · additive · 2 copies · chains A

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
18430.770.81115empty
25100.710.8167empty
31820.490.7625empty
4550.490.8616EDO
51630.480.7722empty

Interfaces

1 interface between chains.

  • A–B · 655 Ų buried · 8 hydrogen bonds · protein-protein

Modifications

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

Compared structures

  • 5ZOY · Copper amine oxidase from Arthrobacter globiformis anaerobically reduced by ethylamine at… · the same entry in another collection · chain A against A, TM-score 1.00

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