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Structure of PHD1 in complex with 1,2,4-triazolo-[1,5-A]PYRIDINE

Analyse Structure of PHD1 in complex with 1,2,4-triazolo-[1,5-A]PYRIDINE in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5V1B
Type
protein
Length
226 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Egl nine homolog 2
EC
1.14.11.29
UniProt
Q96KS0
Ligands
8UY, FE, SO4
Pockets
1 · best druggability 0.68

Structure

x-ray diffraction · 1 distinct chain · 29% helix, 27% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AEgl nine homolog 2 (EC 1.14.11.29)protein22629% helix, 27% strandQ96KS0

Ligands and binding sites

  • 8UY · 4-([1,2,4]triazolo[1,5-a]pyridin-5-yl)benzonitrile · ligand · chains A
  • FE · Fe (III) ion · metal · chains A
  • SO4 · Sulfate ion · ion · 2 copies · 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
14070.680.8047SO4, 8UY

Compared structures

  • 5V1B · Structure of PHD1 in complex with 1,2,4-Triazolo-[1,5-a]pyridine · the same entry in another collection · chain A against A, TM-score 1.00
  • Q96KS0 · AlphaFold monomer V2.0 prediction for prolyl hydroxylase EGLN2 (Q96KS0) · a predicted model of the same protein · chain A against A, TM-score 0.90

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