Structure of PDB 8fsi Chain A

Receptor sequence

>8fsiA (length=245) Species: 83333 (Escherichia coli K-12)

EVIGRIHSFESCGTVDGPGIRFITFFQGCLMRCLYCHNRDTWDTHGGKEV
TVKDLMKEVVTYRHFMNASGGGVTASGGEAILQAEFVRDWFRECKKEGIH
TCLDTNGFVRHYDPVIDELLEVTDLVMLDLKQMNDEIHKNLVGVSNHRTL
RFAQYLAEKNVKVWIRYVVVPGWSDDDDSAHRLGEFTRDMGNVEKIELLP
YHELGKHKWVAMGEEYKLDGVEPPRAETMRRVKGILEQYGHKVMF

3D structure

• PDB: 8fsi Computational engineering of previously crystallized pyruvate formate-lyase activating enzyme reveals insights into SAM binding and reductive cleavage.
• Chain: A
• Resolution: 1.46 Å

Enzymatic activity

• Enzyme Commision number: 1.97.1.4: [formate-C-acetyltransferase]-activating enzyme.

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	SF4	A	C29 M31 C33 C36 W42 G78 N106 K131	C29 M31 C33 C36 W42 G78 N106 K131
BS02	SAM	A	Y35 H37 G77 G78 E79 D104 T105 D129 K131 V168 H202	Y35 H37 G77 G78 E79 D104 T105 D129 K131 V168 H202

Gene Ontology

Molecular Function

• GO:0003824 catalytic activity
• GO:0005515 protein binding
• GO:0016491 oxidoreductase activity
• GO:0030955 potassium ion binding
• GO:0043365 [formate-C-acetyltransferase]-activating enzyme activity
• GO:0046872 metal ion binding
• GO:0051536 iron-sulfur cluster binding
• GO:0051539 4 iron, 4 sulfur cluster binding

Biological Process

• GO:0006006 glucose metabolic process
• GO:0006974 DNA damage response
• GO:0051604 protein maturation

Cellular Component

• GO:0005737 cytoplasm
• GO:0005829 cytosol

External links

• PDB: RCSB:8fsi, PDBe:8fsi, PDBj:8fsi
• PDBsum: 8fsi
• PubMed: 37156396
• UniProt: P0A9N4|PFLA_ECOLI Pyruvate formate-lyase 1-activating enzyme (Gene Name=pflA)