Structure of PDB 4xb6 Chain D

Receptor sequence
>4xb6D (length=277) Species: 511145 (Escherichia coli str. K-12 substr. MG1655) [Search protein sequence]
ANLSGYNFAYLDEQTKRMIRRAILKAVAIPGYQVPFGGREMPMPYGWGTG
GIQLTASVIGESDVLKVIDQGADDTTNAVSIRNFFKRVTGVNTTERTDDA
TVIQTRHRIPETPLTEDQIIIFQVPIPEPLRFIEPRETETRTMHALEEYG
VMQVKLYEDIARFGHIATTYAYPVKVNGRYVMDPSPIPKFDNPKMDMMPA
LQLFGAGREKRIYAVPPFTRVESLDFDDHPFTVQQWDEPCAICGSTHSYL
DEVVLDDAGNRMFVCSDTDYCRQQSEA
3D structure
PDB4xb6 Structural insights into the bacterial carbon-phosphorus lyase machinery.
ChainD
Resolution1.7 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) G32 C241 C244 C266 C272
Catalytic site (residue number reindexed from 1) G31 C240 C243 C265 C271
Enzyme Commision number 4.7.1.1: alpha-D-ribose 1-methylphosphonate 5-phosphate C-P-lyase.
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 ZN D C241 C244 C266 C272 C240 C243 C265 C271
Gene Ontology
Molecular Function
GO:0005515 protein binding
GO:0016829 lyase activity
GO:0046872 metal ion binding
GO:0051539 4 iron, 4 sulfur cluster binding
GO:0098848 alpha-D-ribose 1-methylphosphonate 5-phosphate C-P-lyase activity
Biological Process
GO:0015716 organic phosphonate transport
GO:0019634 organic phosphonate metabolic process
GO:0019700 organic phosphonate catabolic process
Cellular Component
GO:0061694 alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase complex
GO:1904176 carbon phosphorus lyase complex

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:4xb6, PDBe:4xb6, PDBj:4xb6
PDBsum4xb6
PubMed26280334
UniProtP16688|PHNJ_ECOLI Alpha-D-ribose 1-methylphosphonate 5-phosphate C-P lyase (Gene Name=phnJ)

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