Structure of PDB 2qjc Chain A Binding Site BS01
Receptor Information
>2qjc Chain A (length=222) Species:
5691
(Trypanosoma brucei) [
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YANVVTLPNVTGRVIIVGDIHGCRAQLEDLLRAVSFKQGSDTLVAVGDLV
NKGPDSFGVVRLLKRLGAYSVLGNHDAKLLKLVKKLSLAPLAQSIPTDVE
TYLSQLPHIIRIPAHNVMVAHAGLHPQRPVDRQYEDEVTTMRNLIEKVTL
TATEETNDGGKPWASMWRGPETVVFGHDARRGLQEQYKPLAIGLDSRCVY
GGRLSAAVFPGGCIISVPGWNG
Ligand information
Ligand ID
MN
InChI
InChI=1S/Mn/q+2
InChIKey
WAEMQWOKJMHJLA-UHFFFAOYSA-N
SMILES
Software
SMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Mn+2]
CACTVS 3.341
[Mn++]
Formula
Mn
Name
MANGANESE (II) ION
ChEMBL
DrugBank
DB06757
ZINC
PDB chain
2qjc Chain A Residue 400 [
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Receptor-Ligand Complex Structure
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PDB
2qjc
Structural genomics of protein phosphatases.
Resolution
2.05 Å
Binding residue
(original residue number in PDB)
D26 H28 D55
Binding residue
(residue number reindexed from 1)
D19 H21 D48
Annotation score
1
Enzymatic activity
Enzyme Commision number
3.6.1.41
: bis(5'-nucleosyl)-tetraphosphatase (symmetrical).
Gene Ontology
Molecular Function
GO:0000298
endopolyphosphatase activity
GO:0004722
protein serine/threonine phosphatase activity
GO:0008803
bis(5'-nucleosyl)-tetraphosphatase (symmetrical) activity
GO:0016787
hydrolase activity
GO:0016791
phosphatase activity
GO:0046872
metal ion binding
Biological Process
GO:0006470
protein dephosphorylation
GO:0006798
polyphosphate catabolic 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:2qjc
,
PDBe:2qjc
,
PDBj:2qjc
PDBsum
2qjc
PubMed
18058037
UniProt
Q57U41
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