Structure of PDB 6xz2 Chain B

Receptor sequence
>6xz2B (length=237) Species: 83333 (Escherichia coli K-12) [Search protein sequence]
ATPHINAEMGDFADVVLMPGDPLRAKYIAETFLEDAREVNNVRGMLGFTG
TYKGRKISVMGHGMGIPSCSIYTKELITDFGVKKIIRVGSCGAVLPHVKL
RDVVIGMGACTDSKVNRIRFKDHDFAAIADFDMVRNAVDAAKALGIDARV
GNLFSADLFWSPDGEMFDVMEKYGILGVEMEAAGIYGVAAEFGAKALTIC
TVSDHIRTHEQTTAAERQTTFNDMIKIALESVLLGDK
3D structure
PDB6xz2 Single tryptophan Y160W mutant of homooligomeric E. coli purine nucleoside phosphorylase implies that dimers forming the hexamer are functionally not equivalent.
ChainB
Resolution1.65 Å
3D
structure
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Enzymatic activity
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 B M64 S90 F159 V178 E179 M180 E181 D204 M64 S90 F159 V178 E179 M180 E181 D204
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:6xz2, PDBe:6xz2, PDBj:6xz2
PDBsum6xz2
PubMed34045551
UniProtP0ABP8|DEOD_ECOLI Purine nucleoside phosphorylase DeoD-type (Gene Name=deoD)

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