Structure of PDB 6f4w Chain E

Receptor sequence
>6f4wE (length=233) Species: 210 (Helicobacter pylori) [Search protein sequence]
MTPHINAKIGDFYPQCLLCGDPLRVSYIAKKFLQDAKEITNVRNMLGFSG
KYKGRGISLMGHGMGIASCTIYVTELIKTYQVKELLRIGTCGAISPKVGL
KDIIMATGASTDSKTNRVRFLNHDLSATPDFELSLRAYQTAKRLGIDLKV
GNVFSSDFFYSFETHAFDLMAKYNHLAIEMEAAGLYATAMELNAKALCLC
SVSDHLITKEALSPKERVESFDNMIILALEMMS
3D structure
PDB6f4w Helicobacter pylori purine nucleoside phosphorylase shows new distribution patterns of open and closed active site conformations and unusual biochemical features.
ChainE
Resolution2.293 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 2.4.2.1: purine-nucleoside 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 FMC E H4 R43 H4 R43 MOAD: Kd=2.95uM
BS02 FMC E T90 C91 G92 F159 M180 E181 T90 C91 G92 F159 M180 E181 MOAD: Kd=2.95uM
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0004731 purine-nucleoside 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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Cellular Component
External links
PDB RCSB:6f4w, PDBe:6f4w, PDBj:6f4w
PDBsum6f4w
PubMed29430816
UniProtP56463|DEOD_HELPY Purine nucleoside phosphorylase DeoD-type (Gene Name=deoD)

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