Structure of PDB 2qjc Chain A Binding Site BS01

Receptor Information
>2qjc Chain A (length=222) Species: 5691 (Trypanosoma brucei) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
YANVVTLPNVTGRVIIVGDIHGCRAQLEDLLRAVSFKQGSDTLVAVGDLV
NKGPDSFGVVRLLKRLGAYSVLGNHDAKLLKLVKKLSLAPLAQSIPTDVE
TYLSQLPHIIRIPAHNVMVAHAGLHPQRPVDRQYEDEVTTMRNLIEKVTL
TATEETNDGGKPWASMWRGPETVVFGHDARRGLQEQYKPLAIGLDSRCVY
GGRLSAAVFPGGCIISVPGWNG
Ligand information
Ligand IDMN
InChIInChI=1S/Mn/q+2
InChIKeyWAEMQWOKJMHJLA-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Mn+2]
CACTVS 3.341[Mn++]
FormulaMn
NameMANGANESE (II) ION
ChEMBL
DrugBankDB06757
ZINC
PDB chain2qjc Chain A Residue 400 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB2qjc Structural genomics of protein phosphatases.
Resolution2.05 Å
Binding residue
(original residue number in PDB)
D26 H28 D55
Binding residue
(residue number reindexed from 1)
D19 H21 D48
Annotation score1
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
PDBsum2qjc
PubMed18058037
UniProtQ57U41

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