Structure of PDB 4mln Chain B

Receptor sequence
>4mlnB (length=182) Species: 663362 (uncultured bacterium HF130_AEPn_1) [Search protein sequence]
SLSNSSKVSVLISLLEKSRDLDYIINQLEHSLQCAYFAQRSGADNEMVLA
ALLHDLGHYCNTSFEDMGGYGVWQHEKVGADYLRGLGFSERVACLIEGHV
AAKRYLVSSKASYLKNLSDASRKTLEYQGGPMDEGERRLFEEREDFKDCL
KIRAWDEKGKQTDLKVPGPEHYRKMMEEHLSE
3D structure
PDB4mln Crystal structure of PhnZ in complex with substrate reveals a di-iron oxygenase mechanism for catabolism of organophosphonates.
ChainB
Resolution2.1 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 1.13.11.78: 2-amino-1-hydroxyethylphosphonate dioxygenase (glycine-forming).
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 FE B Y24 H34 H58 D59 D161 Y23 H30 H54 D55 D156
BS02 FE B D59 H80 H104 D55 H75 H99
BS03 ODV B Y24 D59 H62 H80 H104 K108 S126 T129 Q133 R158 Y23 D55 H58 H75 H99 K103 S121 T124 Q128 R153
Gene Ontology
Molecular Function
GO:0016491 oxidoreductase activity
GO:0016787 hydrolase activity
GO:0046872 metal ion binding

View graph for
Molecular Function
External links
PDB RCSB:4mln, PDBe:4mln, PDBj:4mln
PDBsum4mln
PubMed24706911
UniProtD0E8I5|PHNZ_UNCHF 2-amino-1-hydroxyethylphosphonate dioxygenase (glycine-forming) (Gene Name=phnZ)

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