Structure of PDB 4xb6 Chain H

Receptor sequence

>4xb6H (length=277) Species: 511145 (Escherichia coli str. K-12 substr. MG1655)

ANLSGYNFAYLDEQTKRMIRRAILKAVAIPGYQVPFGGREMPMPYGWGTG
GIQLTASVIGESDVLKVIDQGADDTTNAVSIRNFFKRVTGVNTTERTDDA
TVIQTRHRIPETPLTEDQIIIFQVPIPEPLRFIEPRETETRTMHALEEYG
VMQVKLYEDIARFGHIATTYAYPVKVNGRYVMDPSPIPKFDNPKMDMMPA
LQLFGAGREKRIYAVPPFTRVESLDFDDHPFTVQQWDEPCAICGSTHSYL
DEVVLDDAGNRMFVCSDTDYCRQQSEA

3D structure

• PDB: 4xb6 Structural insights into the bacterial carbon-phosphorus lyase machinery.
• Chain: H
• Resolution: 1.7 Å

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	H	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

External links

• PDB: RCSB:4xb6, PDBe:4xb6, PDBj:4xb6
• PDBsum: 4xb6
• PubMed: 26280334
• UniProt: P16688|PHNJ_ECOLI Alpha-D-ribose 1-methylphosphonate 5-phosphate C-P lyase (Gene Name=phnJ)