Structure of PDB 1c3x Chain C

Receptor sequence
>1c3xC (length=266) Species: 40001 (Cellulomonas sp.) [Search protein sequence]
PPLDDPATDPFLVARAAADHIAQATGVEGHDMALVLGSGWGGAAELLGEV
VAEVPTHEIPGFSSVTRSIRVERADGSVRHALVLGSRTHLYEGKGVRAVV
HGVRTAAATGAETLILTNGCGGLNQEWGAGTPVLLSDHINLTARSPLEGP
TFVDLTDVYSPRLRELAHRVDPTLPEGVYAQFPGPHYETPAEVRMAGILG
ADLVGMSTTLEAIAARHCGLEVLGVSLVTNLAAGISPTPLSHAEVIEAGQ
AAGPRISALLADIAKR
3D structure
PDB1c3x Crystal structure of the purine nucleoside phosphorylase (PNP) from Cellulomonas sp. and its implication for the mechanism of trimeric PNPs.
ChainC
Resolution2.4 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) S46 R83 H105 Y107 E108 G135 M222 S223 N246 H258
Catalytic site (residue number reindexed from 1) S38 R67 H89 Y91 E92 G119 M206 S207 N230 H242
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 C S46 R103 N134 S223 S38 R87 N118 S207
BS02 8IG C G135 C136 G137 Y203 E204 G221 M222 T245 G119 C120 G121 Y187 E188 G205 M206 T229
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:0009116 nucleoside metabolic process
Cellular Component
GO:0005737 cytoplasm

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1c3x, PDBe:1c3x, PDBj:1c3x
PDBsum1c3x
PubMed10600382
UniProtP81989|PUNA_CELSP Purine nucleoside phosphorylase (Gene Name=punA)

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