Structure of PDB 7z15 Chain D

Receptor sequence
>7z15D (length=278) Species: 562 (Escherichia coli) [Search protein sequence]
ANLSGYNFAYLDEQTKRMIRRAILKAVAIPGYQVPFGGREMPMPYGWGTG
GIQLTASVIGESDVLKVIDQGADDTTNAVSIRNFFKRVTGVNTTERTDDA
TLIQTRHRIPETPLTEDQIIIFQVPIPEPLRFIEPRETETRTMHALEEYG
VMQVKLYEDIARFGHIATTYAYPVKVNGRYVMDPSPIPKFDNPKMDMMPA
LQLFGAGREKRIYAVPPFTRVESLDFDDHPFTVQQWDEPCAICGSTHSYL
DEVVLDDAGNRMFVCSDTDYCRQQSEAK
3D structure
PDB7z15 Structural remodelling of the carbon-phosphorus lyase machinery by a dual ABC ATPase.
ChainD
Resolution1.93 Å
3D
structure
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Enzymatic activity
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
BS02 I9X D G47 G49 T50 G51 R107 H108 Q124 V125 P126 G208 R209 G46 G48 T49 G50 R106 H107 Q123 V124 P125 G207 R208
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:7z15, PDBe:7z15, PDBj:7z15
PDBsum7z15
PubMed36813778
UniProtP16688|PHNJ_ECOLI Alpha-D-ribose 1-methylphosphonate 5-phosphate C-P lyase (Gene Name=phnJ)

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