Structure of PDB 5mx4 Chain C

Receptor sequence
>5mx4C (length=233) Species: 1145110 (Helicobacter pylori R018c) [Search protein sequence]
MTPHINAKIGDFYPQCLLCGDPLRVSYIAKKFLQDAKEITNVRNMLGFSG
KYKGKGISLMGHGMGIASCTIYVTELIKTYQVKELLRIGTCGAISPKVGL
KDIIMATGASTDSKTNRVRFLNHDLSATPDFELSLRAYQTAKRLGIDLKI
GNVFSSDFFYSFETHAFDLMAQYNHLAIEMEAAGLYATAMELNAKALCLC
SVSDHLITKEALSPKERIESFDNMIILALEMMS
3D structure
PDB5mx4 Structural characterization of purine nucleoside phosphorylase from human pathogen Helicobacter pylori.
ChainC
Resolution2.31 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H4 G20 R24 R43 E75 R87 T90 S203 D204 L206 R217
Catalytic site (residue number reindexed from 1) H4 G20 R24 R43 E75 R87 T90 S203 D204 L206 R217
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 HPA C T90 C91 G92 F159 I178 E179 M180 D204 L206 T90 C91 G92 F159 I178 E179 M180 D204 L206
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0004731 purine-nucleoside phosphorylase activity
GO:0004850 uridine phosphorylase activity
GO:0016757 glycosyltransferase activity
GO:0016763 pentosyltransferase activity
Biological Process
GO:0006139 nucleobase-containing compound metabolic process
GO:0006152 purine nucleoside catabolic process
GO:0009116 nucleoside metabolic process
GO:0009164 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:5mx4, PDBe:5mx4, PDBj:5mx4
PDBsum5mx4
PubMed28336275
UniProtK2JXG0

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