Structure of PDB 1hp0 Chain A

Receptor sequence
>1hp0A (length=319) Species: 5699 (Trypanosoma vivax) [Search protein sequence]
SAKNVVLDHDGNLDDFVAMVLLASNTEKVRLIGALCTDADCFVENGFNVT
GKIMCLMHNNMNLPLFPIGKSAATAVNPFPKEWRCLAKNMDDMPILNIPE
NVELWDKIKAENEKYEGQQLLADLVMNSEEKVTICVTGPLSNVAWCIDKY
GEKFTSKVEECVIMGGAVDVRGNVFLPSTDGTAEWNIYWDPASAKTVFGC
PGLRRIMFSLDSTNTVPVRSPYVQRFGEQTNFLLSILVGTMWAMCTHGYY
AWDALTAAYVVDQKVANVDPVPIDVVVDKQPNEGATVRTDAENYPLTFVA
RNPEAEFFLDMLLRSARAC
3D structure
PDB1hp0 Structure and function of a novel purine specific nucleoside hydrolase from Trypanosoma vivax.
ChainA
Resolution2.1 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 D40 W83 T137 W185 N186 W260 D261
Catalytic site (residue number reindexed from 1) D10 D15 D40 W83 T137 W185 N186 W252 D253
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 T137 D261 D10 D15 T137 D253
BS02 AD3 A N12 D14 D40 W83 M164 N173 E184 N186 Y257 W260 D261 N12 D14 D40 W83 M164 N173 E184 N186 Y249 W252 D253 MOAD: Ki=0.2uM
PDBbind-CN: -logKd/Ki=6.70,Ki=0.2uM
Gene Ontology
Molecular Function
GO:0016798 hydrolase activity, acting on glycosyl bonds
GO:0016799 hydrolase activity, hydrolyzing N-glycosyl compounds
GO:0046872 metal ion binding
Biological Process
GO:0006139 nucleobase-containing compound metabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:1hp0, PDBe:1hp0, PDBj:1hp0
PDBsum1hp0
PubMed11292348
UniProtQ9GPQ4

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