Structure of PDB 5tsq Chain A

Receptor sequence
>5tsqA (length=312) Species: 1448350 (Leishmania braziliensis braziliensis) [Search protein sequence]
PRKIILDCDPGIDDAVAILLAYGNPEIELLAITTVVGNQTLEKVTRNAQL
VADVAGIVGVPIAAGCCKPLVRKVRTAPQIHGETGLGTVSYPSEFKTKLD
KRHAVHLIIELIMSHEPKSITLVPTGGLTNIAMAARLEPRIVERVKEVVL
MGGSCCIGNASPVAEFNIFVDPEAAHIVFNESWDVTMVGLDLTSQALATP
EVLQRVKEVRTKPADFILKILEFYTKVYETQRNTYAKVHDPCAVAYVIDP
TVMTTNRVPVNIELNGELTAGMTVTDFRYPRPEQCHTQVASKLDFSKYWD
LVIDALQRIGDP
3D structure
PDB5tsq Crystal structure of IUnH from Leishmania braziliensis in complex with D-Ribose
ChainA
Resolution1.53 Å
3D
structure
Catalytic site residues are labeled in the structure
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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 3.2.2.1: 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 A D10 D15 T126 D241 D9 D14 T125 D240
BS02 BDR A D14 N39 H82 M152 E166 F167 H240 D241 D13 N38 H81 M151 E165 F166 H239 D240
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
Biological Process
GO:0006139 nucleobase-containing compound metabolic process
GO:0006152 purine nucleoside catabolic process
Cellular Component
GO:0005829 cytosol

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:5tsq, PDBe:5tsq, PDBj:5tsq
PDBsum5tsq
PubMed
UniProtA4H9Q9

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