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Structure of human deoxyhypusine hydroxylase in complex with glycerol

Analyse Structure of human deoxyhypusine hydroxylase in complex with glycerol in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4D4Z
Type
protein
Length
578 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Deoxyhypusine hydroxylase
EC
1.14.99.29
UniProt
Q9BU89
Ligands
FE, OH
Pockets
3 · best druggability 0.71

Structure

x-ray diffraction · 2 distinct chains · 75% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ADeoxyhypusine hydroxylase (EC 1.14.99.29)protein28875% helix, 0% strandQ9BU89
BDeoxyhypusine hydroxylase (EC 1.14.99.29)protein29074% helix, 0% strandQ9BU89

Ligands and binding sites

  • FE · Fe (III) ion · metal · 4 copies · chains A, B
  • OH · Hydroxide ion · ion · 2 copies · chains A, B
  • GOL · Glycerol · additive · 2 copies · chains A, B
  • B3P · 2-[3-(2-hydroxy-1,1-dihydroxymethyl-ethylamino)-propylamino]-2-hydroxymethyl-propane-1,3-diol · additive · chains A

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
17490.710.7884empty
2800.410.7918empty
3850.320.7316empty

Interfaces

1 interface between chains.

  • A–B · 1350 Ų buried · 11 hydrogen bonds · protein-protein

Compared structures

  • 4D4Z · STRUCTURE OF HUMAN DEOXYHYPUSINE HYDROXYLASE in complex with glycerol · the same entry in another collection · chain A against A, TM-score 1.00
  • Q9BU89 · AlphaFold monomer V2.0 prediction for deoxyhypusine hydroxylase (Q9BU89) · a predicted model of the same protein · chain A against A, TM-score 0.98

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