Structure of PDB 4kpn Chain B

Receptor sequence

>4kpnB (length=318) Species: 3218 (Physcomitrium patens)

PPKKVIIDTDPGIDDAMAIFFALKSPELDVIALTTIYGNVRTPTATVNAL
HLLEFAGREDIPVSEGFRTSLRGELKERIADFVHGADGLGNTYPTLSDRK
PIDTFAPDYLIQKVNEFPGEITIVALGPLTNLAAAVECDPTFAKKVGQII
ILGGAFQVNGNVNPAAEANIYGDPEAADIIFTCGADILVVGINITHQVYW
TGKDLEDLGRSDSKFGKYLYAASHFYATYHREAYDIDAIYLHDPATMVAA
VDPSLMTYATGAVRVQKDGICKGLTLFNNSNKVWHDPTDWCGIPPVKVAV
TVDRERVASLLKERLTAP

3D structure

• PDB: 4kpn Structure and Function of Nucleoside Hydrolases from Physcomitrella patens and Maize Catalyzing the Hydrolysis of Purine, Pyrimidine, and Cytokinin Ribosides.
• Chain: B
• Resolution: 3.35 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): D25 D30 N54 L141 A183 N184 H257 D258
• Catalytic site (residue number reindexed from 1): D10 D15 N39 L126 A168 N169 H242 D243
• Enzyme Commision number: 3.2.2.1: purine nucleosidase.

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	CA	B	D25 D30 L141 D258	D10 D15 L126 D243

Gene Ontology

Molecular Function

• GO:0008477 purine nucleosidase activity
• GO:0016798 hydrolase activity, acting on glycosyl bonds
• GO:0016799 hydrolase activity, hydrolyzing N-glycosyl compounds
• GO:0035251 UDP-glucosyltransferase activity
• GO:0046872 metal ion binding
• GO:0046982 protein heterodimerization activity
• GO:0047724 inosine nucleosidase activity

Biological Process

• GO:0006139 nucleobase-containing compound metabolic process
• GO:0006148 inosine catabolic process
• GO:0006152 purine nucleoside catabolic process
• GO:0010150 leaf senescence

Cellular Component

• GO:0005829 cytosol

External links

• PDB: RCSB:4kpn, PDBe:4kpn, PDBj:4kpn
• PDBsum: 4kpn
• PubMed: 24170203
• UniProt: A9TXA6