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Arginine hydroxylase vioc in complex with (3S)-oh-arg, succinate and fe after oxygen exposure using ft-ssx methods

Analyse Arginine hydroxylase vioc in complex with (3S)-oh-arg, succinate and fe after… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6Y12
Type
protein
Length
330 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Alpha-ketoglutarate-dependent L-arginine hydroxylase
EC
1.14.11.41
UniProt
Q6WZB0
Ligands
ZZU, FE
Pockets
6 · best druggability 0.74

Structure

x-ray diffraction · 1 distinct chain · 32% helix, 23% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AAlpha-ketoglutarate-dependent L-arginine hydroxylase (EC 1.14.11.41)protein33032% helix, 23% strandQ6WZB0

Ligands and binding sites

  • ZZU · (2S,3S)-3-hydroxyarginine · ligand · chains A
  • FE · Fe (III) ion · metal · chains A
  • SIN · Succinic acid · additive · chains A

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1940.740.9627SIN, ZZU
2670.500.8520empty
31190.420.7624empty
4610.360.7814empty
5690.320.7515empty

Compared structures

  • 6Y12 · Arginine hydroxylase VioC in complex with (3S)-OH-Arg, succinate and Fe after oxygen… · the same entry in another collection · chain A against A, TM-score 1.00
  • Q6WZB0 · AlphaFold monomer V2.0 prediction for alpha-ketoglutarate-dependent L-arginine… · a predicted model of the same protein · chain A against A, TM-score 1.00

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