Structure of PDB 7z18 Chain D

Receptor sequence

>7z18D (length=278) Species: 562 (Escherichia coli)

ANLSGYNFAYLDEQTKRMIRRAILKAVAIPGYQVPFGGREMPMPYGWGTG
GIQLTASVIGESDVLKVIDQGADDTTNAVSIRNFFKRVTGVNTTERTDDA
TLIQTRHRIPETPLTEDQIIIFQVPIPEPLRFIEPRETETRTMHALEEYG
VMQVKLYEDIARFGHIATTYAYPVKVNGRYVMDPSPIPKFDNPKMDMMPA
LQLFGAGREKRIYAVPPFTRVESLDFDDHPFTVQQWDEPCAICGSTHSYL
DEVVLDDAGNRMFVCSDTDYCRQQSEAK

3D structure

• PDB: 7z18 Structural remodelling of the carbon-phosphorus lyase machinery by a dual ABC ATPase.
• Chain: D
• Resolution: 1.98 Å

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	Y46 G47 W48 G49 T50 G51 R107 H108 Q124 V125 P126 G208 R209	Y45 G46 W47 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

External links

• PDB: RCSB:7z18, PDBe:7z18, PDBj:7z18
• PDBsum: 7z18
• PubMed: 36813778
• UniProt: P16688|PHNJ_ECOLI Alpha-D-ribose 1-methylphosphonate 5-phosphate C-P lyase (Gene Name=phnJ)