Structure of PDB 4dan Chain A

Receptor sequence

>4danA (length=229) Species: 1423 (Bacillus subtilis)

SVHIGAEKGQIADTVLLPGDPLRAKFIAETYLENVECYNEVRGMYGFTGT
YKGKKISVQGTGMGVPSISIYVNELIQSYDVQNLIRVGSCGAIRKDVKVR
DVILAMTSSTDSQMNRVAFGSVDFAPCADFELLKNAYDAAKDKGVPVTVG
SVFTADQFYNDDSQIEKLAKYGVLGVEMETTALYTLAAKHGRKALSILTV
SDHVLTGEETTAEERQTTFHDMIDVALHS

3D structure

• PDB: 4dan Insights into phosphate cooperativity and influence of substrate modifications on binding and catalysis of hexameric purine nucleoside phosphorylases.
• Chain: A
• Resolution: 2.56 Å

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 S201 D202 V204 R215
• 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	2FA	A	S90 C91 G92 F159 V177 E178 M179 E180 S202	S89 C90 G91 F158 V176 E177 M178 E179 S201
BS02	2FA	A	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

External links

• PDB: RCSB:4dan, PDBe:4dan, PDBj:4dan
• PDBsum: 4dan
• PubMed: 22957058
• UniProt: O34925|DEOD_BACSU Purine nucleoside phosphorylase DeoD-type (Gene Name=deoD)