Structure of PDB 2amx Chain B Binding Site BS02
Receptor Information
>2amx Chain B (length=356) Species:
5861
(Plasmodium yoelii) [
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GLVPRGSEIKFLKKEDVQNIDLNGMSKKERYEIWRRIPKVELHCHLDLTF
SAEFFLKWARKYNLQPNMSDDEILDHYLFTKEGKSLAEFIRKAISVSDLY
RDYDFIEDLAKWAVIEKYKEGVVLMEFRYSPTFVSSSYGLDVELIHKAFI
KGIKNATELLNNKIHVALICISDKHSGDFAIKHKHDFVGFDHGGREIDLK
DHKDVYHSVRDHGLHLTVHAGEDATLPNLNTLYTAINILNVERIGHGIRV
SESDELIELVKKKDILLEVCPISNLLLNNVKSMDTHPIRKLYDAGVKVSV
NSDDPGMFLSNINDNYEKLYIHLNFTLEEFMIMNNWAFEKSFVSDDVKSE
LKALYF
Ligand information
Ligand ID
CO
InChI
InChI=1S/Co/q+2
InChIKey
XLJKHNWPARRRJB-UHFFFAOYSA-N
SMILES
Software
SMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Co+2]
CACTVS 3.341
[Co++]
Formula
Co
Name
COBALT (II) ION
ChEMBL
DrugBank
DB14205
ZINC
PDB chain
2amx Chain B Residue 1001 [
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Receptor-Ligand Complex Structure
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PDB
2amx
Genome-scale protein expression and structural biology of Plasmodium falciparum and related Apicomplexan organisms.
Resolution
2.02 Å
Binding residue
(original residue number in PDB)
H212 H222
Binding residue
(residue number reindexed from 1)
H192 H202
Annotation score
1
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
PDBsum
2amx
PubMed
17125854
UniProt
Q7RMV2
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