Structure of PDB 3ooe Chain E

Receptor sequence
>3ooeE (length=227) Species: 83333 (Escherichia coli K-12) [Search protein sequence]
ATPHINAEMGDFADVVLMPGDPLRAKYIAETFLEDAREVNNVRGMLGFTG
TYKGRKISVMGHGMGIPSCSIYTKELITDFGVKKIIRVGSCGAVLPHVKL
RDVVIGMGACTDSKVNRIRFKDHDFAAIADFDMVRNAVDAAKALGIDARV
GNLFSADLFYSPDGEMFDVMEKYGILGVEMEAAGIYGVAAEFGAKALTIC
TVSDHIRTTTFNDMIKIALESVLLGDK
3D structure
PDB3ooe Validation of the catalytic mechanism of Escherichia coli purine nucleoside phosphorylase by structural and kinetic studies.
ChainE
Resolution2.0 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 S90 S203 D204 I206
Catalytic site (residue number reindexed from 1) H4 G20 R24 R43 E75 R87 S90 S203 D204 I206
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 PO4 E G20 R87 S90 G20 R87 S90
BS02 PO4 E T220 N222 T210 N212
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0004731 purine-nucleoside phosphorylase activity
GO:0016757 glycosyltransferase activity
GO:0016763 pentosyltransferase activity
GO:0042802 identical protein binding
GO:0047975 guanosine phosphorylase activity
Biological Process
GO:0006139 nucleobase-containing compound metabolic process
GO:0006152 purine nucleoside catabolic process
GO:0006974 DNA damage response
GO:0009116 nucleoside metabolic process
GO:0009164 nucleoside catabolic process
GO:0019686 purine nucleoside interconversion
GO:0042278 purine nucleoside metabolic process
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol
GO:0016020 membrane

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Molecular Function
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Cellular Component
External links
PDB RCSB:3ooe, PDBe:3ooe, PDBj:3ooe
PDBsum3ooe
PubMed21672603
UniProtP0ABP8|DEOD_ECOLI Purine nucleoside phosphorylase DeoD-type (Gene Name=deoD)

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