Structure of PDB 1n77 Chain B Binding Site BS02

Receptor Information
>1n77 Chain B (length=468) Species: 274 (Thermus thermophilus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MVVTRIAPSPTGDPHVGTAYIALFNYAWARRNGGRFIVRIEDTDRARYVP
GAEERILAALKWLGLSYDEGPDVGGPHGPYRQSERLPLYQKYAEELLKRG
WAYRAFETPEELEQIRKEKGGYDGRARNIPPEEAEERARRGEPHVIRLKV
PRPGTTEVKDELRGVVVYDNQEIPDVVLLKSDGYPTYHLANVVDDHLMGV
TDVIRAEEWLVSTPIHVLLYRAFGWEAPRFYHMPLLRNPDKTKISKRKSH
TSLDWYKAEGFLPEALRNYLCLMGFSMPDGREIFTLEEFIQAFTWERVSL
GGPVFDLEKLRWMNGKYIREVLSLEEVAERVKPFLREAGLSWESEAYLRR
AVELMRPRFDTLKEFPEKARYLFTEDYPVSEKAQRKLEEGLPLLKELYPR
LRAQEEWTEAALEALLRGFAAEKGVKLGQVAQPLRAALTGSLETPGLFEI
LALLGKERALRRLERALA
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 chain1n77 Chain B Residue 601 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB1n77 ATP binding by glutamyl-tRNA synthetase is switched to the productive mode by tRNA binding
Resolution2.4 Å
Binding residue
(original residue number in PDB)		H15 I21 A206 E208 W209 L235
Binding residue
(residue number reindexed from 1)		H15 I21 A206 E208 W209 L235
Annotation score5
Enzymatic activity
Catalytic site (original residue number in PDB) K246
Catalytic site (residue number reindexed from 1) K246
Enzyme Commision number 6.1.1.17: glutamate--tRNA ligase.
Gene Ontology
Molecular Function
GO:0000049 tRNA binding
GO:0000166 nucleotide binding
GO:0004812 aminoacyl-tRNA ligase activity
GO:0004818 glutamate-tRNA ligase activity
GO:0005524 ATP binding
GO:0008270 zinc ion binding
Biological Process
GO:0006412 translation
GO:0006418 tRNA aminoacylation for protein translation
GO:0006424 glutamyl-tRNA aminoacylation
GO:0043039 tRNA aminoacylation
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1n77, PDBe:1n77, PDBj:1n77
PDBsum1n77
PubMed12554668
UniProtP27000|SYE_THET8 Glutamate--tRNA ligase (Gene Name=gltX)

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