Structure of PDB 4d9h Chain B

Receptor sequence
>4d9hB (length=229) Species: 1423 (Bacillus subtilis) [Search protein sequence]
SVHIGAEKGQIADTVLLPGDPLRAKFIAETYLENVECYNEVRGMYGFTGT
YKGKKISVQGTGMGVPSISIYVNELIQSYDVQNLIRVGSCGAIRKDVKVR
DVILAMTSSTDSQMNRVAFGSVDFAPCADFELLKNAYDAAKDKGVPVTVG
SVFTADQFYDSQIEKLAKYGVLGVEMETTALYTLAAKHGRKALSILTVSD
HVLTGEETTAEERQTTFHDMIDVALHSVS
3D structure
PDB4d9h Insights into phosphate cooperativity and influence of substrate modifications on binding and catalysis of hexameric purine nucleoside phosphorylases.
ChainB
Resolution1.91 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 S202 D203 V205 R216
Catalytic site (residue number reindexed from 1) H3 G19 R23 R42 E74 R86 S89 S199 D200 V202 R213
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 ADN B H4 R43 H3 R42
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
GO:0042278 purine nucleoside metabolic 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:4d9h, PDBe:4d9h, PDBj:4d9h
PDBsum4d9h
PubMed22957058
UniProtO34925|DEOD_BACSU Purine nucleoside phosphorylase DeoD-type (Gene Name=deoD)

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