Structure of PDB 1ezr Chain D

Receptor sequence

>1ezrD (length=312) Species: 5664 (Leishmania major)

PRKIILDCDPGIDDAVAIFLAHGNPEIELLAITTVVGNQSLEKVTQNARL
VADVAGIVGVPVAAGCTKPLVRGVRNASHIHGETGMGNVSYPPEFKTKLD
GRHAVQLIIDLIMSHEPKTITLVPTGGLTNIAMAVRLEPRIVDRVKEVVL
MGGGYHTGNASPVAEFNVFIDPEAAHIVFNESWNVTMVGLDLTHLALATP
AVQKRVREVGTKPAAFMLQILDFYTKVYEKEHDTYGKVHDPCAVAYVIDP
TVMTTERVPVDIELNGALTTGMTVADFRYPRPKNCRTQVAVKLDFDKFWC
LVIDALERIGDP

3D structure

• PDB: 1ezr Nucleoside hydrolase from Leishmania major. Cloning, expression, catalytic properties, transition state inhibitors, and the 2.5-a crystal structure.
• Chain: D
• Resolution: 2.5 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): D10 D15 N39 V75 T126 F167 N168 H240 D241
• Catalytic site (residue number reindexed from 1): D9 D14 N38 V74 T125 F166 N167 H239 D240
• 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	D	D10 D15 T126 D241	D9 D14 T125 D240

Gene Ontology

Molecular Function

• GO:0005509 calcium ion binding
• 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:0009117 nucleotide metabolic process
• GO:0043101 purine-containing compound salvage

Cellular Component

• GO:0005575 cellular_component

External links

• PDB: RCSB:1ezr, PDBe:1ezr, PDBj:1ezr
• PDBsum: 1ezr
• PubMed: 10409664
• UniProt: P83851|IUNH_LEIMA Inosine-uridine preferring nucleoside hydrolase (Gene Name=NSNH)