Structure of PDB 1yns Chain A Binding Site BS01

Receptor Information

>1yns Chain A (length=254) Species: 9606 (Homo sapiens)

LSVPAEVTVILLDIEGTTTPIAFVKDILFPYIEENVKEYLQTHWEEEECQ
QDVSLLRKQAEEDAHLDGAVPIPAASGNGVDDLQQMIQAVVDNVCWQMSL
DRKTTALKQLQGHMWRAAFTAGRMKAEFFADVVPAVRKWREAGMKVYIYS
SGSVEAQKLLFGHSTEGDILELVDGHFDTKIGHKVESESYRKIADSIGCS
TNNILFLTDVTREASAAEEADVHVAVVVRPGNAGLTDDEKTYYSLITSFS
ELYL

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: 1yns Chain A Residue 1258

Receptor-Ligand Complex Structure

Structure summary

• PDB: 1yns Crystal structure of human e1 enzyme and its complex with a substrate analog reveals the mechanism of its phosphatase/enolase
• Resolution: 1.7 Å
• Binding residue (original residue number in PDB): D16 E18 D212
• Binding residue (residue number reindexed from 1): D13 E15 D209
• Annotation score: 1

Enzymatic activity

• Enzyme Commision number: 3.1.3.77: acireductone synthase.

Gene Ontology

Molecular Function

• GO:0000287 magnesium ion binding
• GO:0005515 protein binding
• GO:0016787 hydrolase activity
• GO:0043715 2,3-diketo-5-methylthiopentyl-1-phosphate enolase activity
• GO:0043716 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate phosphatase activity
• GO:0043874 acireductone synthase activity
• GO:0046872 metal ion binding

Biological Process

• GO:0009086 methionine biosynthetic process
• GO:0019284 L-methionine salvage from S-adenosylmethionine
• GO:0019509 L-methionine salvage from methylthioadenosine

Cellular Component

• GO:0005634 nucleus
• GO:0005737 cytoplasm
• GO:0005829 cytosol

External links

• PDB: RCSB:1yns, PDBe:1yns, PDBj:1yns
• PDBsum: 1yns
• PubMed: 15843022
• UniProt: Q9UHY7|ENOPH_HUMAN Enolase-phosphatase E1 (Gene Name=ENOPH1)