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Lysine-N,N-dimethylated hif prolyl hydroxylase 2 (PHD2/ EGLN1) in complex with bb-287

Analyse Lysine-N,N-dimethylated hif prolyl hydroxylase 2 (PHD2/ EGLN1) in complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6YW0
Type
protein
Length
222 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Egl nine homolog 1
EC
1.14.11.29
UniProt
Q9GZT9
Ligands
2JP, BCT, FE
Pockets
1 · best druggability 0.62

Structure

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

ChainMoleculeTypeResiduesSecondary structureUniProt
AEgl nine homolog 1 (EC 1.14.11.29)protein22230% helix, 30% strandQ9GZT9

Ligands and binding sites

  • 2JP · 4-(isoquinolin-3-ylamino)-4-oxobutanoic acid · ligand · chains A
  • BCT · Bicarbonate ion · 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

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11280.620.8621FE, 2JP

Modifications

Observed in the structure: 17 modified, 1 disulfide (methylation, disulfide).

Compared structures

  • 6YW0 · Lysine-N,N-Dimethylated HIF prolyl hydroxylase 2 (PHD2/ EGLN1) in complex with BB-287 · 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 0.92

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