Structure of PDB 2mas Chain B

Receptor sequence

>2masB (length=313) Species: 5656 (Crithidia fasciculata)

AKKIILDCDPGLDDAVAILLAHGNPEIELLAITTVVGNQTLAKVTRNAQL
VADIAGITGVPIAAGCDKPLVRKIMTAGHIHGESGMGTVAYPAEFKNKVD
ERHAVNLIIDLVMSHEPKTITLVPTGGLTNIAMAARLEPRIVDRVKEVVL
MGGGYHEGNATSVAEFNIIIDPEAAHIVFNESWQVTMVGLDLTHQALATP
PILQRVKEVDTNPARFMLEIMDYYTKIYQSNRYMAAAAVHDPCAVAYVID
PSVMTTERVPVDIELTGKLTLGMTVADFRNPRPEHCHTQVAVKLDFEKFW
GLVLDALERIGDP

3D structure

• PDB: 2mas Trypanosomal nucleoside hydrolase. A novel mechanism from the structure with a transition-state inhibitor.
• Chain: B
• Resolution: 2.3 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): D10 D15 N39 I75 T126 F167 N168 H241 D242
• Catalytic site (residue number reindexed from 1): D9 D14 N38 I74 T125 F166 N167 H240 D241
• Enzyme Commision number: 3.2.2.2: inosine nucleosidase.
  3.2.2.3: uridine 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	D10 D15 T126 D242	D9 D14 T125 D241
BS02	PIR	B	D14 N39 I81 H82 M152 E166 N168 D242	D13 N38 I80 H81 M151 E165 N167 D241	MOAD: Kd=30nM

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:0045437 uridine nucleosidase activity
• GO:0046872 metal ion binding
• GO:0047724 inosine nucleosidase activity

Biological Process

• GO:0006139 nucleobase-containing compound metabolic process
• GO:0006152 purine nucleoside catabolic process
• GO:0009117 nucleotide metabolic process

Cellular Component

• GO:0005829 cytosol

External links

• PDB: RCSB:2mas, PDBe:2mas, PDBj:2mas
• PDBsum: 2mas
• PubMed: 9572842
• UniProt: Q27546|IUNH_CRIFA Inosine-uridine preferring nucleoside hydrolase (Gene Name=IUNH)