Structure of PDB 7f3v Chain B

Receptor sequence

>7f3vB (length=241) Species: 562 (Escherichia coli)

KLIVPQWPQPKGVAACSSTRIGGVSLPPYDSLNLGAHCGDNPDHVEENRK
RLFAAGNLPSKPVWLEQVHGKDVLKLTGEPYASKRADASYSNTPGTVCAV
MTADALPVLFCNRAGTEVAAAHAGWRGLCAGVLEETVSCFADNPENILAW
LGPAIGPRAFEVGGEVREAFMAVDAKASAAFIQHGDKYLADIYQLARQRL
ANVGVEQIFGGDRCTYTENETFFSYRRDKTTGRMASFIWLI

3D structure

• PDB: 7f3v Structural Basis for the Peptidoglycan-Editing Activity of YfiH.
• Chain: B
• 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	B	H71 T104 A105 A107 H124 G126 W127 R128 E163 V164 G165 K189 Y227 R228	H69 T102 A103 A105 H122 G124 W125 R126 E161 V162 G163 K187 Y225 R226

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)