Structure of PDB 6qxl Chain C Binding Site BS02

Receptor Information

>6qxl Chain C (length=483) Species: 287 (Pseudomonas aeruginosa)

MSVRRTKIVATLGPASNSPEVLEQLILAGIDVARLNFSHGTPDEHRARAR
LVRELAAKHGRFVALLGDLQGPKIRIAKFANKRIELQVGDKFRFSTSHAR
DAGTQEVVGIDYPDLVKDCGVGDELLLDDGRVVMVVEEVAADELRCRVLI
GGPLSDHKGINRRGGGLTAPALTDKDKADIKLAADMDLDYVAVSFPRDAK
DMEYARRLLTEAGGKAWLVAKIERAEAVADDDALDGLIRASDAVMVARGD
LGVEIGDAELVGIQKKIILHARRNNKVVITATQMMESMIHSPMPTRAEVS
DVANAVLDYTDAVMLSAESAAGEYPVEAVKAMARVCQGAEKHPTSQKSSH
RLGQTFDRCDESIALASMYTANHFPGIKAIICLTESGFTPLIMSRIRSSV
PIYAYSPHRETQARVAMFRGVETIPFDPAALPAEKVSQAAVDELLKRGVV
TKGDWVILTKGDSYTAQGGTNTMKVLHVGDLLV

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: 6qxl Chain C Residue 502

Receptor-Ligand Complex Structure

Structure summary

• PDB: 6qxl Evolutionary plasticity in the allosteric regulator-binding site of pyruvate kinase isoform PykA fromPseudomonas aeruginosa.
• Resolution: 2.43 Å
• Binding residue (original residue number in PDB): K73 E223 D250
• Binding residue (residue number reindexed from 1): K73 E223 D250
• Annotation score: 1

Enzymatic activity

• Catalytic site (original residue number in PDB): R34 R75 K221 T282
• Catalytic site (residue number reindexed from 1): R34 R75 K221 T282
• Enzyme Commision number: 2.7.1.40: pyruvate kinase.

Gene Ontology

Molecular Function

• GO:0000287 magnesium ion binding
• GO:0003824 catalytic activity
• GO:0004743 pyruvate kinase activity
• GO:0005524 ATP binding
• GO:0016301 kinase activity
• GO:0030955 potassium ion binding
• GO:0046872 metal ion binding

Biological Process

• GO:0006096 glycolytic process
• GO:0016310 phosphorylation

Cellular Component

• GO:0005737 cytoplasm
• GO:0005829 cytosol

External links

• PDB: RCSB:6qxl, PDBe:6qxl, PDBj:6qxl
• PDBsum: 6qxl
• PubMed: 31484721
• UniProt: Q9HW72