Structure of PDB 2amx Chain B Binding Site BS02

Receptor Information
>2amx Chain B (length=356) Species: 5861 (Plasmodium yoelii) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
GLVPRGSEIKFLKKEDVQNIDLNGMSKKERYEIWRRIPKVELHCHLDLTF
SAEFFLKWARKYNLQPNMSDDEILDHYLFTKEGKSLAEFIRKAISVSDLY
RDYDFIEDLAKWAVIEKYKEGVVLMEFRYSPTFVSSSYGLDVELIHKAFI
KGIKNATELLNNKIHVALICISDKHSGDFAIKHKHDFVGFDHGGREIDLK
DHKDVYHSVRDHGLHLTVHAGEDATLPNLNTLYTAINILNVERIGHGIRV
SESDELIELVKKKDILLEVCPISNLLLNNVKSMDTHPIRKLYDAGVKVSV
NSDDPGMFLSNINDNYEKLYIHLNFTLEEFMIMNNWAFEKSFVSDDVKSE
LKALYF
Ligand information
Ligand IDCO
InChIInChI=1S/Co/q+2
InChIKeyXLJKHNWPARRRJB-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Co+2]
CACTVS 3.341[Co++]
FormulaCo
NameCOBALT (II) ION
ChEMBL
DrugBankDB14205
ZINC
PDB chain2amx Chain B Residue 1001 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB2amx Genome-scale protein expression and structural biology of Plasmodium falciparum and related Apicomplexan organisms.
Resolution2.02 Å
Binding residue
(original residue number in PDB)
H212 H222
Binding residue
(residue number reindexed from 1)
H192 H202
Annotation score1
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.
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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