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Crystal structure of topaquinone-containing amine oxidase activated by cobalt ion

Analyse Crystal structure of topaquinone-containing amine oxidase activated by cobalt… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1WMN
Type
protein
Length
1,240 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Phenylethylamine oxidase
EC
1.4.3.6
UniProt
P46881
Ligands
CO
Pockets
15 · best druggability 0.90

Structure

x-ray diffraction · 1 distinct chain · 11% helix, 43% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BPhenylethylamine oxidase (EC 1.4.3.6)protein62011% helix, 43% strandP46881

Ligands and binding sites

  • CO · Cobalt (II) ion · metal · 2 copies · chains A, B

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

Pockets

15 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
110730.900.92142empty
23280.720.8552empty
32990.710.8552empty
42220.670.8428empty
53100.640.8036empty

Interfaces

1 interface between chains.

  • A–B · 6786 Ų buried · 108 hydrogen bonds · protein-protein

Modifications

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

Compared structures

  • 1WMN · Crystal structure of topaqui -containing amine oxidase activated by cobalt ion · the same entry in another collection · chain A against A, TM-score 1.00

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