Structure of PDB 2p4s Chain B

Receptor sequence
>2p4sB (length=282) Species: 7165 (Anopheles gambiae) [Search protein sequence]
YTYDTLQEIATYLLERTELRPKVGIICGSGLGTLAEQLTDVDSFDYETIP
HFPVSTVAGHVGRLVFGYLAGVPVMCMQGRFHHYEGYPLAKCAMPVRVMH
LIGCTHLIATNAAGGANPKYRVGDIMLIKDHINLMGFAGNNPLQGPNDER
FGPRFFGMANTYDPKLNQQAKVIARQIGIENELREGVYTCLGGPNFETVA
EVKMLSMLGVDAIGMSTVHEIITARHCGMTCFAFSLITNMCTMSYEEEEE
HCHDSIVGVGKNREKTLGEFVSRIVKHIHYEA
3D structure
PDB2p4s Anopheles gambiae purine nucleoside phosphorylase: catalysis, structure, and inhibition.
ChainB
Resolution2.2 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) S118 H149 H171 Y173 E174 A201 M304 S305 N328 C330 H342
Catalytic site (residue number reindexed from 1) S29 H60 H82 Y84 E85 A112 M215 S216 N239 C241 H253
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 B G117 S118 R169 H171 N200 S305 G28 S29 R80 H82 N111 S216
BS02 DIH B H171 Y173 A201 A202 G203 F285 E286 I302 M304 N328 H342 H82 Y84 A112 A113 G114 F196 E197 I213 M215 N239 H253 MOAD: Ki=0.31nM
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0004731 purine-nucleoside phosphorylase activity
GO:0016757 glycosyltransferase activity
Biological Process
GO:0006139 nucleobase-containing compound metabolic process
GO:0006166 purine ribonucleoside salvage
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:2p4s, PDBe:2p4s, PDBj:2p4s
PDBsum2p4s
PubMed17918964
UniProtA4Q998|PNPH_ANOGA Purine nucleoside phosphorylase (Gene Name=pnp)

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