Structure of PDB 2amx Chain B

Receptor sequence
>2amxB (length=356) Species: 5861 (Plasmodium yoelii) [Search protein sequence]
GLVPRGSEIKFLKKEDVQNIDLNGMSKKERYEIWRRIPKVELHCHLDLTF
SAEFFLKWARKYNLQPNMSDDEILDHYLFTKEGKSLAEFIRKAISVSDLY
RDYDFIEDLAKWAVIEKYKEGVVLMEFRYSPTFVSSSYGLDVELIHKAFI
KGIKNATELLNNKIHVALICISDKHSGDFAIKHKHDFVGFDHGGREIDLK
DHKDVYHSVRDHGLHLTVHAGEDATLPNLNTLYTAINILNVERIGHGIRV
SESDELIELVKKKDILLEVCPISNLLLNNVKSMDTHPIRKLYDAGVKVSV
NSDDPGMFLSNINDNYEKLYIHLNFTLEEFMIMNNWAFEKSFVSDDVKSE
LKALYF
3D structure
PDB2amx Genome-scale protein expression and structural biology of Plasmodium falciparum and related Apicomplexan organisms.
ChainB
Resolution2.02 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H55 H57 H239 E242 H266 D323
Catalytic site (residue number reindexed from 1) H43 H45 H219 E222 H246 D303
Enzyme Commision number 3.5.4.4: adenosine deaminase.
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 CO B H55 H57 H239 D323 H43 H45 H219 D303
BS02 CO B H212 H222 H192 H202
BS03 CO B N174 H177 E370 N162 H165 E350
Gene Ontology
Molecular Function
GO:0004000 adenosine deaminase activity
GO:0019239 deaminase activity
Biological Process
GO:0006154 adenosine catabolic process
GO:0006166 purine ribonucleoside salvage
GO:0009168 purine ribonucleoside monophosphate biosynthetic process
GO:0043103 hypoxanthine salvage
GO:0046103 inosine biosynthetic process
GO:0060169 negative regulation of adenosine receptor signaling pathway
Cellular Component
GO:0005829 cytosol
GO:0009897 external side of plasma membrane

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:2amx, PDBe:2amx, PDBj:2amx
PDBsum2amx
PubMed17125854
UniProtQ7RMV2

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