Structure of PDB 7f3v Chain C

Receptor sequence

>7f3vC (length=238) Species: 562 (Escherichia coli)

SKLIVPQWPQPKGVAACSSTRIGGVSLPPYDSLNLGAHCGDNPDHVEENR
KRLFAAGNLPSKPVWLEQVHGKDVLKLTGSKRADASYSNTPGTVCAVMTA
DALPVLFCNRAGTEVAAAHAGWRGLCAGVLEETVSCFADNPENILAWLGP
AIGPRAFEVGGEVREAFMAVDAKASAAFIQHGDKYLADIYQLARQRLANV
GVEQIFGGDRCTYTENETFFSYRRDKTTGRMASFIWLI

3D structure

• PDB: 7f3v Structural Basis for the Peptidoglycan-Editing Activity of YfiH.
• Chain: C
• Resolution: 1.47 Å

Enzymatic activity

• Enzyme Commision number: 1.10.3.-
  2.4.2.1: purine-nucleoside phosphorylase.
  2.4.2.28: S-methyl-5'-thioadenosine phosphorylase.
  3.5.4.4: adenosine deaminase.

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	EPZ	C	H71 T104 A105 A107 H124 G126 W127 R128 E163 V164 G165 E167 V168 K189 Y227 R228	H70 T99 A100 A102 H119 G121 W122 R123 E158 V159 G160 E162 V163 K184 Y222 R223

Gene Ontology

Molecular Function

• GO:0004000 adenosine deaminase activity
• GO:0004731 purine-nucleoside phosphorylase activity
• GO:0005507 copper ion binding
• GO:0016491 oxidoreductase activity
• GO:0016682 oxidoreductase activity, acting on diphenols and related substances as donors, oxygen as acceptor
• GO:0016740 transferase activity
• GO:0016787 hydrolase activity
• GO:0017061 S-methyl-5-thioadenosine phosphorylase activity
• GO:0042803 protein homodimerization activity
• GO:0046872 metal ion binding
• GO:0046936 2'-deoxyadenosine deaminase activity

Biological Process

• GO:0000270 peptidoglycan metabolic process

Cellular Component

• GO:0005829 cytosol
• GO:0030288 outer membrane-bounded periplasmic space

External links

• PDB: RCSB:7f3v, PDBe:7f3v, PDBj:7f3v
• PDBsum: 7f3v
• PubMed: 35164571
• UniProt: P33644|PURNU_ECOLI Purine nucleoside phosphorylase YfiH (Gene Name=yfiH)