Structure of PDB 4mln Chain A Binding Site BS03

Receptor Information

>4mln Chain A (length=182) Species: 663362 (uncultured bacterium HF130_AEPn_1)

LSNSSKVSVLISLLEKSRDLDYIGEAINQLEHSLQCAYFAQRSGADNEMV
LAALLHDLGHYCNDTSFEDMGGYGVWQHEKVGADYLRGLGFSERVACLIE
GHVAAKRYLVSSKYLKNLSDASRKTLEYQGGPMDGERRLFEEREDFKDCL
KIRAWDEKGKQTDLKVPGPEHYRKMMEEHLSE

Ligand information

• Ligand ID: ODV
• InChI: InChI=1S/C2H8NO4P/c3-1-2(4)8(5,6)7/h2,4H,1,3H2,(H2,5,6,7)/t2-/m1/s1
• InChIKey: RTTXIBKRJFIBBG-UWTATZPHSA-N
• SMILES:
  CACTVS 3.385: NC[CH](O)[P](O)(O)=O
  CACTVS 3.385: NC[C@H](O)[P](O)(O)=O
  ACDLabs 12.01: O=P(O)(O)C(O)CN
  OpenEye OEToolkits 1.7.6: C([C@H](O)P(=O)(O)O)N
  OpenEye OEToolkits 1.7.6: C(C(O)P(=O)(O)O)N
• Formula: C2 H8 N O4 P
• Name: [(1R)-2-amino-1-hydroxyethyl]phosphonic acid
• ZINC: ZINC000019204143
• PDB chain: 4mln Chain A Residue 203

Receptor-Ligand Complex Structure

Structure summary

• PDB: 4mln Crystal structure of PhnZ in complex with substrate reveals a di-iron oxygenase mechanism for catabolism of organophosphonates.
• Resolution: 2.1 Å
• Binding residue (original residue number in PDB): D59 H80 H104 K108 S126 T129 R158
• Binding residue (residue number reindexed from 1): D57 H78 H102 K106 S122 T125 R153
• Annotation score: 5

Enzymatic activity

• Enzyme Commision number: 1.13.11.78: 2-amino-1-hydroxyethylphosphonate dioxygenase (glycine-forming).

Gene Ontology

Molecular Function

• GO:0016491 oxidoreductase activity
• GO:0016787 hydrolase activity
• GO:0046872 metal ion binding

External links

• PDB: RCSB:4mln, PDBe:4mln, PDBj:4mln
• PDBsum: 4mln
• PubMed: 24706911
• UniProt: D0E8I5|PHNZ_UNCHF 2-amino-1-hydroxyethylphosphonate dioxygenase (glycine-forming) (Gene Name=phnZ)