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L-Amino acid oxidase/monooxygenase from Pseudomonas sp. AIU 813 - L-arginine complex

Analyse L-Amino acid oxidase/monooxygenase from Pseudomonas sp. AIU 813 - L-arginine… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5YB8
Type
protein
Length
2,196 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v2 / PDB Bank
Contract
0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner
0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution
2.3
Source
Pseudomonas sp. AIU 813
Molecule
L-amino acid oxidase/monooxygenase
UniProt
W6JQJ6
Ligands
ARG, FAD
Pockets
20 · best druggability 0.88

Structure

x-ray diffraction · resolution 2.3 · 1 distinct chain · 36% helix, 20% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, DL-amino acid oxidase/monooxygenaseprotein54936% helix, 20% strandW6JQJ6

Ligands and binding sites

  • ARG · Arginine · ligand · 8 copies · chains A, D, B, C
  • FAD · Flavin-adenine dinucleotide · ligand · 4 copies · chains A, B, C, D

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

Pockets

20 pockets found on a 1 Å grid, 18 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
18530.880.91103empty
211650.880.89123ARG
37110.860.90103ARG, FAD
46880.860.9095ARG, FAD
57130.860.90100ARG, FAD

Interfaces

4 interfaces between chains.

  • A–D · 1904 Ų buried · 22 hydrogen bonds · protein-protein
  • B–C · 1837 Ų buried · 18 hydrogen bonds · protein-protein
  • A–B · 1517 Ų buried · 21 hydrogen bonds · protein-protein
  • C–D · 1510 Ų buried · 22 hydrogen bonds · protein-protein

Compared structures

  • 5YB8 · L-amino acid OXIDASE/MONOOXYGENASE from pseudomonas sp. aiu 813 - L- arginine complex · the same entry in another collection · chain A against A, TM-score 1.00

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