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Human JMJD5 in complex with mn and 5-((2-METHOXYBENZYL)AMINO)PYRIDINE- 2,4-dicarboxylic acid.

Analyse Human JMJD5 in complex with mn and 5-((2-METHOXYBENZYL)AMINO)PYRIDINE… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7DYW
Type
protein
Length
236 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Bifunctional peptidase and arginyl-hydroxylase JMJD5
EC
1.14.11.-, 3.4.-.-
UniProt
Q8N371
Ligands
HRL, MN
Pockets
1 · best druggability 0.64

Structure

x-ray diffraction · 1 distinct chain · 25% helix, 33% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ABifunctional peptidase and arginyl-hydroxylase JMJD5 (EC 1.14.11.-, 3.4.-.-)protein23625% helix, 33% strandQ8N371

Ligands and binding sites

  • HRL · 5-((2-methoxybenzyl)amino)pyridine-2,4-dicarboxylic acid · ligand · chains A
  • MN · Manganese (II) 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
13980.640.7842HRL, MN

Compared structures

  • 7DYW · Human JMJD5 in complex with MN and 5-((2-methoxybenzyl)amino)pyridine-2,4-dicarboxylic… · the same entry in another collection · chain A against A, TM-score 1.00
  • Q8N371 · AlphaFold monomer V2.0 prediction for bifunctional peptidase and arginyl-hydroxylase… · a predicted model of the same protein · chain A against A, TM-score 0.98

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