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The crystal structure of augmenter of liver regeneration: a mammalian FAD dependent sulfhydryl oxidase

Analyse The crystal structure of augmenter of liver regeneration: a mammalian FAD… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1OQC
Type
protein
Length
447 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Augmenter of liver regeneration
UniProt
Q63042
Ligands
FAD
Pockets
4 · best druggability 0.75

Structure

x-ray diffraction · 2 distinct chains · 67% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, C, DAugmenter of liver regenerationprotein11267% helix, 0% strandQ63042
BAugmenter of liver regenerationprotein11168% helix, 0% strandQ63042

Ligands and binding sites

  • 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

4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
19570.750.7891FAD
22820.650.8139FAD
32300.620.8139FAD
4540.260.7317empty

Interfaces

3 interfaces between chains.

  • A–C · 1496 Ų buried · 11 hydrogen bonds · protein-protein
  • B–D · 1448 Ų buried · 11 hydrogen bonds · protein-protein
  • B–C · 163 Ų buried · 0 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 12 disulfide (disulfide).

Compared structures

  • 1OQC · The crystal structure of augmenter of liver regeneration: a mammalian FAD dependent… · the same entry in another collection · chain A against A, TM-score 1.00
  • Q63042 · AlphaFold monomer V2.0 prediction for FAD-linked sulfhydryl oxidase alr (Q63042) · a predicted model of the same protein · chain D against A, TM-score 0.99

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