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Arginine hydroxylase vioc in complex with arg, 2OG and fe under anaerobic environment using ft-ssx methods

Analyse Arginine hydroxylase vioc in complex with arg, 2OG and fe under anaerobic… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6Y0N
Type
protein
Length
327 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
ARG, AKG, FE
Pockets
5 · best druggability 0.77

Structure

x-ray diffraction · 1 distinct chain · 31% helix, 22% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AAlpha-ketoglutarate-dependent L-arginine hydroxylase (EC 1.14.11.41)protein32731% helix, 22% strandQ6WZB0

Ligands and binding sites

  • ARG · Arginine · ligand · chains A
  • AKG · 2-oxoglutaric acid · ligand · chains A
  • FE · Fe (III) ion · metal · chains A

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11050.770.9723ARG, AKG, FE
2610.510.8617empty
3580.340.7716empty
4740.330.7520empty
5650.310.7417empty

Compared structures

  • 6Y0N · Arginine hydroxylase VioC in complex with Arg, 2OG and Fe under anaerobic environment… · 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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