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Structure of Prolyl Hydroxylase Domain-containing Protein (PHD) with Inhibitors

Analyse Structure of Prolyl Hydroxylase Domain-containing Protein (PHD) with Inhibitors in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4JZR
Type
protein
Length
204 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v2 / PDB Bank
Contract
0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner
0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution
2.1
Source
Homo sapiens
Molecule
Egl nine homolog 1
EC
1.14.11.29
UniProt
Q9GZT9
Ligands
4JR, NI
Pockets
1 · best druggability 0.64

Structure

x-ray diffraction · resolution 2.1 · 1 distinct chain · 27% helix, 30% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AEgl nine homolog 1 (EC 1.14.11.29)protein20427% helix, 30% strandQ9GZT9

Ligands and binding sites

  • 4JR · 2-(biphenyl-4-yl)-8-[(1-methyl-1H-imidazol-2-yl)methyl]-2,8-diazaspiro[4.5]decan-1-one · ligand · chains A
  • NI · Nickel (II) ion · metal · chains A
  • EDO · 1,2-ethanediol · additive · chains A

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11280.640.8723NI, 4JR, EDO

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

  • 4JZR · Structure of prolyl hydroxylase domain-containing protein (phd) with inhibitors · the same entry in another collection · chain A against A, TM-score 1.00
  • Q9GZT9 · AlphaFold monomer V2.0 prediction for egl nine homolog 1 (Q9GZT9) · a predicted model of the same protein · chain A against A, TM-score 0.97

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