Structure of PDB 3al0 Chain C Binding Site BS02

Receptor Information
>3al0 Chain C (length=564) Species: 243274 (Thermotoga maritima MSB8) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
KVTKDLVLHLENLARLELSEDQRESLMKDFQEILDYVELLNEVDVEGVEP
MYTPVEDSAKLRKGDPRFFEMRDLIKKNFPEEKDGHIKVPGIPKKIRRCF
ELVRVRFAPSPTGHLHVGGARTALFNWMFARKEGGKFILRIEDTDTERSS
REYEQQILESLRWCGLDWDEGPDIGGDFGPYRQSERLEIYREYAEKLVED
KRAYYVVYDKEDPSKELFTTYEYPHEYKEKGHPVTIKFKVLPGKTSFEDL
LKGYMEFDNSTLEDFIIMKSNGFPTYNFAVVVDDHLMRISHVFRGEDHLS
NTPKQLMIYEAFGWEAPVFMHIPLILGSDRTPLSKRHGATSVEHFRREGI
LSRALMNYLALLGWRVEGDEIFTIEEKLQSFDPKDISNKGVIFDYQKLEW
VNGKHMRRIDLEDLKREFIEWAKYAGKEIPSVDERYFSETLRICREKVNT
LSQLYDIMYPFMNDDYEYEKDYVEKFLKREEAERVLEEAKKAFKDLNSWN
MEEIEKTLRDLSEKGLASKKVVFQLIRGAVTGKLVTPGLFETIEVLGKER
TLKRLERTLQFLKK
Ligand information
Ligand IDGSU
InChIInChI=1S/C15H21N7O9S/c16-6(1-2-8(23)24)14(27)21-32(28,29)30-3-7-10(25)11(26)15(31-7)22-5-20-9-12(17)18-4-19-13(9)22/h4-7,10-11,15,25-26H,1-3,16H2,(H,21,27)(H,23,24)(H2,17,18,19)/t6-,7+,10+,11+,15+/m0/s1
InChIKeyYBRKRYFZKHICLS-WERHYGNASA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0c1nc(c2c(n1)n(cn2)C3C(C(C(O3)COS(=O)(=O)NC(=O)C(CCC(=O)O)N)O)O)N
CACTVS 3.341N[C@@H](CCC(O)=O)C(=O)N[S](=O)(=O)OC[C@H]1O[C@H]([C@H](O)[C@@H]1O)n2cnc3c(N)ncnc23
OpenEye OEToolkits 1.5.0c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)COS(=O)(=O)NC(=O)[C@H](CCC(=O)O)N)O)O)N
CACTVS 3.341N[CH](CCC(O)=O)C(=O)N[S](=O)(=O)OC[CH]1O[CH]([CH](O)[CH]1O)n2cnc3c(N)ncnc23
ACDLabs 10.04O=C(O)CCC(N)C(=O)NS(=O)(=O)OCC3OC(n2cnc1c(ncnc12)N)C(O)C3O
FormulaC15 H21 N7 O9 S
NameO5'-(L-GLUTAMYL-SULFAMOYL)-ADENOSINE
ChEMBLCHEMBL1163071
DrugBank
ZINCZINC000014967046
PDB chain3al0 Chain C Residue 1001 [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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PDB3al0 Two enzymes bound to one transfer RNA assume alternative conformations for consecutive reactions.
Resolution3.368 Å
Binding residue
(original residue number in PDB)		R132 A134 P135 G144 T148 E168 Y302 R320 G321 D323 H324 L350 I351 L359
Binding residue
(residue number reindexed from 1)		R106 A108 P109 G118 T122 E142 Y276 R294 G295 D297 H298 L324 I325 L333
Annotation score2
Enzymatic activity
Catalytic site (original residue number in PDB) S136 K361
Catalytic site (residue number reindexed from 1) S110 K335
Enzyme Commision number 6.1.1.17: glutamate--tRNA ligase.
6.3.5.-
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
GO:0016874 ligase activity
GO:0050566 asparaginyl-tRNA synthase (glutamine-hydrolyzing) activity
GO:0050567 glutaminyl-tRNA synthase (glutamine-hydrolyzing) activity
Biological Process
GO:0006412 translation
GO:0006418 tRNA aminoacylation for protein translation
GO:0006424 glutamyl-tRNA aminoacylation
GO:0006450 regulation of translational fidelity
GO:0043039 tRNA aminoacylation
GO:0070681 glutaminyl-tRNAGln biosynthesis via transamidation
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol

View graph for
Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:3al0, PDBe:3al0, PDBj:3al0
PDBsum3al0
PubMed20882017
UniProtQ9WY94;
Q9X2I8|SYE2_THEMA Glutamate--tRNA ligase 2 (Gene Name=gltX2)

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