Structure of PDB 2q0e Chain A Binding Site BS01

Receptor Information
>2q0e Chain A (length=331) Species: 5691 (Trypanosoma brucei) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
PSPAVVGRSLVNSFKQFVSKDLHTRHVDATYRLVLDCVAAVDPLMRLYTF
GSTVVYGVHEKGSDVDFVVLNKTDVEDGKGGDAATQVAKGLQADILAKLA
RVIRQKHLSWNVEEVRRTRVPVVRVKGGGAVDFDITAYRRNGVRNSALLR
AYFEQNPPCRWLSMSIKRWSKQTGLNASVIGGSITSYGFNLMVVYYLLQR
NHLQFVPPSTIDVSRVEPLPPHLPLEEPADEGLELGTQVLDFLHFFLHEF
DSDKQVISLNRPGITTKEELDWTKSAEDFARMNGEKVHYQWCIEDPYELN
LNVGRNVTPLKRDFLRRHLEKARDTALLTIV
Ligand information
Ligand IDMG
InChIInChI=1S/Mg/q+2
InChIKeyJLVVSXFLKOJNIY-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Mg+2]
CACTVS 3.341[Mg++]
FormulaMg
NameMAGNESIUM ION
ChEMBL
DrugBankDB01378
ZINC
PDB chain2q0e Chain A Residue 401 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB2q0e Dual role of the RNA substrate in selectivity and catalysis by terminal uridylyl transferases.
Resolution2.1 Å
Binding residue
(original residue number in PDB)
D66 D68
Binding residue
(residue number reindexed from 1)
D64 D66
Annotation score1
Enzymatic activity
Enzyme Commision number 2.7.7.52: RNA uridylyltransferase.
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0003723 RNA binding
GO:0016779 nucleotidyltransferase activity
GO:0046872 metal ion binding
GO:0050265 RNA uridylyltransferase activity
Biological Process
GO:0071076 RNA 3' uridylation
Cellular Component
GO:0005737 cytoplasm
GO:0005739 mitochondrion
GO:0020023 kinetoplast

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:2q0e, PDBe:2q0e, PDBj:2q0e
PDBsum2q0e
PubMed17785418
UniProtQ381M1|TUT4_TRYB2 Terminal uridylyltransferase 4 (Gene Name=TUT4)

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