Structure of PDB 2q0d Chain A Binding Site BS02

Receptor Information
>2q0d Chain A (length=325) Species: 5691 (Trypanosoma brucei) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
PSPAVVGRSLVNSFKQFVSHVDATYRLVLDCVAAVDPLMRLYTFGSTVVY
GVHEKGSDVDFVVLNKTDVEDGKGGDAATQVAKGLQADILAKLARVIRQK
HLSWNVEEVRRTRVPVVRVKGGGAVDFDITAYRRNGVRNSALLRAYFEQN
PPCRWLSMSIKRWSKQTGLNASVIGGSITSYGFNLMVVYYLLQRNHLQFV
PPSTIDVSRVEPLPPHLPLEEPADEGLELGTQVLDFLHFFLHEFDSDKQV
ISLNRPGITTKEELDWTKSAEDFARMNGEKVHYQWCIEDPYELNLNVGRN
VTPLKRDFLRRHLEKARDTALLTIV
Ligand information
Ligand IDATP
InChIInChI=1S/C10H16N5O13P3/c11-8-5-9(13-2-12-8)15(3-14-5)10-7(17)6(16)4(26-10)1-25-30(21,22)28-31(23,24)27-29(18,19)20/h2-4,6-7,10,16-17H,1H2,(H,21,22)(H,23,24)(H2,11,12,13)(H2,18,19,20)/t4-,6-,7-,10-/m1/s1
InChIKeyZKHQWZAMYRWXGA-KQYNXXCUSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0c1nc(c2c(n1)n(cn2)C3C(C(C(O3)COP(=O)(O)OP(=O)(O)OP(=O)(O)O)O)O)N
CACTVS 3.341Nc1ncnc2n(cnc12)[CH]3O[CH](CO[P](O)(=O)O[P](O)(=O)O[P](O)(O)=O)[CH](O)[CH]3O
ACDLabs 10.04O=P(O)(O)OP(=O)(O)OP(=O)(O)OCC3OC(n2cnc1c(ncnc12)N)C(O)C3O
OpenEye OEToolkits 1.5.0c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)CO[P@@](=O)(O)O[P@](=O)(O)OP(=O)(O)O)O)O)N
CACTVS 3.341Nc1ncnc2n(cnc12)[C@@H]3O[C@H](CO[P@](O)(=O)O[P@@](O)(=O)O[P](O)(O)=O)[C@@H](O)[C@H]3O
FormulaC10 H16 N5 O13 P3
NameADENOSINE-5'-TRIPHOSPHATE
ChEMBLCHEMBL14249
DrugBankDB00171
ZINCZINC000004261765
PDB chain2q0d Chain A Residue 501 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB2q0d Dual role of the RNA substrate in selectivity and catalysis by terminal uridylyl transferases.
Resolution2.0 Å
Binding residue
(original residue number in PDB)		F52 G53 S54 S65 D68 R121 N147 K169 K173 T187 S188 Y189 V305 R307
Binding residue
(residue number reindexed from 1)		F44 G45 S46 S57 D60 R113 N139 K161 K165 T179 S180 Y181 V297 R299
Annotation score2
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

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:2q0d, PDBe:2q0d, PDBj:2q0d
PDBsum2q0d
PubMed17785418
UniProtQ381M1|TUT4_TRYB2 Terminal uridylyltransferase 4 (Gene Name=TUT4)

[Back to BioLiP]