Structure of PDB 2fea Chain A Binding Site BS02

Receptor Information

>2fea Chain A (length=225) Species: 1423 (Bacillus subtilis)

TRKPFIICDFDGTITMNDNIINIMKTFAPPEWMALKDGVLSKTLSIKEGV
GRMFGLLPSSLKEEITSFVLEDAKIREGFREFVAFINEHEIPFYVISGGM
DFFVYPLLEGIVEKDRIYCNHASFDNDYIHIDWPHSCKGTCSNQCGCCKP
SVIHELSEPNQYIIMIGDSVTDVEAAKLSDLCFARDYLLNECREQNLNHL
PYQDFYEIRKEIENVKEVQEWLQNK

Ligand information

• Ligand ID: ZN
• InChI: InChI=1S/Zn/q+2
• InChIKey: PTFCDOFLOPIGGS-UHFFFAOYSA-N
• SMILES:
  CACTVS 3.341: [Zn++]
  ACDLabs 10.04
  OpenEye OEToolkits 1.5.0: [Zn+2]
• Formula: Zn
• Name: ZINC ION
• ChEMBL: CHEMBL1236970
• DrugBank: DB14532
• PDB chain: 2fea Chain A Residue 1302

Receptor-Ligand Complex Structure

Structure summary

• PDB: 2fea Crystal structure of MtnX phosphatase from Bacillus subtilis at 2.0 A resolution provides a structural basis for bipartite phosphomonoester hydrolysis of 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate.
• Resolution: 2.0 Å
• Binding residue (original residue number in PDB): C139 C143 C147 C150
• Binding residue (residue number reindexed from 1): C137 C141 C145 C148
• Annotation score: 1

Enzymatic activity

• Enzyme Commision number: 3.1.3.87: 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate phosphatase.

Gene Ontology

Molecular Function

• GO:0008253 5'-nucleotidase activity
• GO:0016787 hydrolase activity
• GO:0016791 phosphatase activity
• GO:0043716 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate phosphatase activity

Biological Process

• GO:0009086 methionine biosynthetic process
• GO:0019509 L-methionine salvage from methylthioadenosine
• GO:0071267 L-methionine salvage

Cellular Component

• GO:0005737 cytoplasm

External links

• PDB: RCSB:2fea, PDBe:2fea, PDBj:2fea
• PDBsum: 2fea
• PubMed: 17654724
• UniProt: O31667|MTNX_BACSU 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate phosphatase (Gene Name=mtnX)