Structure of PDB 5zfx Chain B Binding Site BS02

Receptor Information

>5zfx Chain B (length=248) Species: 6198 (Opisthorchis viverrini)

RKFFVGGNWKMNGSKKENDKLIEMLTHAKIDPNTEVLVAPPALYLPSVRE
KLDKRFHVAAQNCYKVPSGAFTGEVSPAMLKDVGCDWVILGHSERRHILL
ETDQLVGEKTNHAISAGVNVIACIGEKLEEREAGKTEEVCFRQMEAIRKN
LSSADMWNHIVIAYEPVWAIGTGKTATEQQAQEVHLAVRRWMEEKVSPAV
AKSIRIIYGGSVTAANCRTLAKQPDVDGFLVGGASLKPDFIEICNANA

Ligand information

• Ligand ID: MG
• InChI: InChI=1S/Mg/q+2
• InChIKey: JLVVSXFLKOJNIY-UHFFFAOYSA-N
• SMILES:
  ACDLabs 10.04
  OpenEye OEToolkits 1.5.0: [Mg+2]
  CACTVS 3.341: [Mg++]
• Formula: Mg
• Name: MAGNESIUM ION
• DrugBank: DB01378
• PDB chain: 5zfx Chain B Residue 302

Receptor-Ligand Complex Structure

Structure summary

• PDB: 5zfx Structural Analysis of an Epitope Candidate of Triosephosphate Isomerase in Opisthorchis viverrini.
• Resolution: 1.751 Å
• Binding residue (original residue number in PDB): A173 T176 K178
• Binding residue (residue number reindexed from 1): A169 T172 K174
• Annotation score: 1

Enzymatic activity

• Catalytic site (original residue number in PDB): N12 K14 H96 E98 E169 G175 S215
• Catalytic site (residue number reindexed from 1): N8 K10 H92 E94 E165 G171 S211
• Enzyme Commision number: 5.3.1.1: triose-phosphate isomerase.

Gene Ontology

Molecular Function

• GO:0004807 triose-phosphate isomerase activity
• GO:0016853 isomerase activity
• GO:0046872 metal ion binding

Biological Process

• GO:0006094 gluconeogenesis
• GO:0006096 glycolytic process
• GO:0019563 glycerol catabolic process
• GO:0046166 glyceraldehyde-3-phosphate biosynthetic process

Cellular Component

• GO:0005829 cytosol

External links

• PDB: RCSB:5zfx, PDBe:5zfx, PDBj:5zfx
• PDBsum: 5zfx
• PubMed: 30305716
• UniProt: A0A074Z863