Structure of PDB 2orw Chain B Binding Site BS02

Receptor Information
>2orw Chain B (length=173) Species: 2336 (Thermotoga maritima) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
SGKLTVITGPMYSGKTTELLSFVEIYKLGKKKVAVFKPKIDTMIVSHGVE
AHVIERPEEMRKYIEEDTRGVFIDEVQFFNPSLFEVVKDLLDRGIDVFCA
GLDLTHKQNPFETTALLLSLADTVIKKKAVCHRCGEYNATLTLKVAGGEE
EIDVGGQEKYIAVCRDCYNTLKK
Ligand information
Ligand ID4TA
InChIInChI=1S/C20H29N7O20P4/c1-8-3-26(20(32)25-18(8)31)12-2-9(28)10(43-12)4-41-48(33,34)45-50(37,38)47-51(39,40)46-49(35,36)42-5-11-14(29)15(30)19(44-11)27-7-24-13-16(21)22-6-23-17(13)27/h3,6-7,9-12,14-15,19,28-30H,2,4-5H2,1H3,(H,33,34)(H,35,36)(H,37,38)(H,39,40)(H2,21,22,23)(H,25,31,32)/p-4/t9-,10+,11+,12+,14+,15+,19+/m0/s1
InChIKeyWLGHSSFVEUABFP-SLFMBYJQSA-J
SMILES
SoftwareSMILES
CACTVS 3.385CC1=CN([CH]2C[CH](O)[CH](CO[P]([O-])(=O)O[P]([O-])(=O)O[P]([O-])(=O)O[P]([O-])(=O)OC[CH]3O[CH]([CH](O)[CH]3O)n4cnc5c(N)ncnc45)O2)C(=O)NC1=O
OpenEye OEToolkits 1.7.5CC1=CN(C(=O)NC1=O)[C@H]2C[C@@H]([C@H](O2)COP(=O)([O-])OP(=O)([O-])OP(=O)([O-])OP(=O)([O-])OC[C@@H]3[C@H]([C@H]([C@@H](O3)n4cnc5c4ncnc5N)O)O)O
OpenEye OEToolkits 1.7.5CC1=CN(C(=O)NC1=O)C2CC(C(O2)COP(=O)([O-])OP(=O)([O-])OP(=O)([O-])OP(=O)([O-])OCC3C(C(C(O3)n4cnc5c4ncnc5N)O)O)O
CACTVS 3.385CC1=CN([C@H]2C[C@H](O)[C@@H](CO[P]([O-])(=O)O[P]([O-])(=O)O[P]([O-])(=O)O[P]([O-])(=O)OC[C@H]3O[C@H]([C@H](O)[C@@H]3O)n4cnc5c(N)ncnc45)O2)C(=O)NC1=O
FormulaC20 H25 N7 O20 P4
NameP1-(5'-ADENOSYL)P4-(5'-(2'-DEOXY-THYMIDYL))TETRAPHOSPHATE
ChEMBL
DrugBank
ZINC
PDB chain2orw Chain B Residue 802 [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]
PDB2orw Binding of ATP to TK1-like Enzymes Is Associated with a Conformational Change in the Quaternary Structure.
Resolution1.5 Å
Binding residue
(original residue number in PDB)		M12 Y13 G15 K16 T17 T18 S52 E84 F87 L111 T114 H115 A138 V139 T151 E160 D162 V163 G164 Y169
Binding residue
(residue number reindexed from 1)		M11 Y12 G14 K15 T16 T17 S46 E75 F78 L102 T105 H106 A129 V130 T142 E151 D153 V154 G155 Y160
Annotation score3
Enzymatic activity
Enzyme Commision number 2.7.1.21: thymidine kinase.
Gene Ontology
Molecular Function
GO:0004797 thymidine kinase activity
GO:0005524 ATP binding
GO:0008270 zinc ion binding
GO:0016301 kinase activity
GO:0042802 identical protein binding
GO:0046872 metal ion binding
Biological Process
GO:0006259 DNA metabolic process
GO:0009157 deoxyribonucleoside monophosphate biosynthetic process
GO:0016310 phosphorylation
GO:0046104 thymidine metabolic process
GO:0071897 DNA biosynthetic process
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:2orw, PDBe:2orw, PDBj:2orw
PDBsum2orw
PubMed17407781
UniProtQ9WYN2|KITH_THEMA Thymidine kinase (Gene Name=tdk)

[Back to BioLiP]