Structure of PDB 3pug Chain A Binding Site BS02

Receptor Information

>3pug Chain A (length=349) Species: 309800 (Haloferax volcanii DS2)

TERRHDREFVRTFFTSPTAVEDDSAKMLRRAAGLRGMQAPDVWVPDNEDA
TAPSMRDEGAENIVEVISEQGAEFPGEIHPRMVWHRDSPETRYQGFQHML
DITDPERGAVEHIHGFVIPEVGGIDDWKKADEFFTIVEHEHGLDEGSLAM
SVIIESGEAELAMGDLRDEMGKPTNNLERLFLLVDGEVDYTKDMRAMTPT
GELPAWPELRHNTSRGASAAGCVAVDGPYDDIRDVEGYRERMTDNQAKGM
LGIWSLTPGQVVEANTSPLPPKTGSWLLDEELLGLTSYVPSMDDIVDSME
EFEWDEATYQAAMTPISLFQDVYENRPDQHEELEERYGAGVVERAMEVG

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: 3pug Chain A Residue 601

Receptor-Ligand Complex Structure

Structure summary

• PDB: 3pug Crystal structures of a halophilic archaeal malate synthase from Haloferax volcanii and comparisons with isoforms A and G.
• Resolution: 2.7 Å
• Binding residue (original residue number in PDB): E158 D192
• Binding residue (residue number reindexed from 1): E155 D189
• Annotation score: 1

Enzymatic activity

• Enzyme Commision number: 2.3.3.9: malate synthase.

Gene Ontology

Molecular Function

• GO:0000287 magnesium ion binding
• GO:0003824 catalytic activity
• GO:0004474 malate synthase activity
• GO:0016740 transferase activity
• GO:0046872 metal ion binding

Biological Process

• GO:0006097 glyoxylate cycle
• GO:0006099 tricarboxylic acid cycle
• GO:0006107 oxaloacetate metabolic process

Cellular Component

• GO:0005737 cytoplasm

External links

• PDB: RCSB:3pug, PDBe:3pug, PDBj:3pug
• PDBsum: 3pug
• PubMed: 21569248
• UniProt: D4GTL2|ACEB_HALVD Malate synthase (Gene Name=aceB)