Structure of PDB 3pns Chain H

Receptor sequence
>3pnsH (length=249) Species: 243277 (Vibrio cholerae O1 biovar El Tor str. N16961) [Search protein sequence]
TVFHLGVTEADLNGATLAIIPGDPARVQKIAELMDNPVFLASHREYTVYR
AELDGQSVVVCSTGIGGPSTSIAVEELAQLGVRTFLRVGTTGAIQPHVNV
GDMIVTTGSVRLDGASLHFAPMEFPAVPDFDVATAMKAAAQESGATVHMG
VTASSDTFYPGQERYDTFTGRVVRRFQGSMKEWQDMGVLNFEMESATLLT
MCASSGLKAGCVAGVIINRTQKEIPDHATLKETEARSIKVVVEAARKML
3D structure
PDB3pns Crystal Structure of Uridine Phosphorylase Complexed with Uracil from Vibrio cholerae O1 biovar El Tor
ChainH
Resolution2.002 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H12 G30 R34 R52 E84 R95 T98 R172 I224 I225 R227 L238
Catalytic site (residue number reindexed from 1) H4 G22 R26 R44 E76 R87 T90 R164 I216 I217 R219 L230
Enzyme Commision number 2.4.2.3: uridine phosphorylase.
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 URA H T99 G100 F166 Q170 I225 T91 G92 F158 Q162 I217
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0004850 uridine phosphorylase activity
GO:0016757 glycosyltransferase activity
GO:0016763 pentosyltransferase activity
GO:0047847 deoxyuridine phosphorylase activity
Biological Process
GO:0009116 nucleoside metabolic process
GO:0009164 nucleoside catabolic process
GO:0009166 nucleotide catabolic process
GO:0044206 UMP salvage
Cellular Component
GO:0005737 cytoplasm
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:3pns, PDBe:3pns, PDBj:3pns
PDBsum3pns
PubMed
UniProtQ9KT71

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