Structure of PDB 1g51 Chain B Binding Site BS01

Receptor Information
>1g51 Chain B (length=580) Species: 274 (Thermus thermophilus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MRRTHYAGSLRETHVGEEVVLEGWVNRRRDLGGLIFLDLRDREGLVQLVA
HPASPAYATAERVRPEWVVRAKGLVRLRPEPNPRLATGRVEVELSALEVL
AEAKTPPFPVDAGWRGEEEKEASEELRLKYRYLDLRRRRMQENLRLRHRV
IKAIWDFLDREGFVQVETPFLTKSTPEGARDFLVPYRHEPGLFYALPQSP
QLFKQMLMVAGLDRYFQIARCFRDEDLRADRQPDFTQLDLEMSFVEVEDV
LELNERLMAHVFREALGVELPLPFPRLSYEEAMERYGSDKPDLRFGLELK
EVGPLFRQSGFRVFQEAESVKALALPKALSRKEVAELEEVAKRHKAQGLA
WARVEEGGFSGGVAKFLEPVREALLQATEARPGDTLLFVAGPRKVAATAL
GAVRLRAADLLGLKREGFRFLWVVDFPLLEWDEEEEAWTYMHHPFTSPHP
EDLPLLEKDPGRVRALAYDLVLNGVEVGGGSIRIHDPRLQARVFRLLGIG
EEEQREKFGFFLEALEYGAPPHGGIAWGLDRLLALMTGSPSIREVIAFPK
NKEGKDPLTGAPSPVPEEQLRELGLMVVRP
Ligand information
Ligand IDAMO
InChIInChI=1S/C14H19N6O10P/c15-5(1-7(21)22)14(25)30-31(26,27)28-2-6-9(23)10(24)13(29-6)20-4-19-8-11(16)17-3-18-12(8)20/h3-6,9-10,13,23-24H,1-2,15H2,(H,21,22)(H,26,27)(H2,16,17,18)/t5-,6+,9+,10+,13+/m0/s1
InChIKeyQPBSGQWTJLPZNF-VWJPMABRSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0c1nc(c2c(n1)n(cn2)C3C(C(C(O3)COP(=O)(O)OC(=O)C(CC(=O)O)N)O)O)N
OpenEye OEToolkits 1.5.0c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)CO[P@](=O)(O)OC(=O)[C@H](CC(=O)O)N)O)O)N
CACTVS 3.341N[CH](CC(O)=O)C(=O)O[P](O)(=O)OC[CH]1O[CH]([CH](O)[CH]1O)n2cnc3c(N)ncnc23
ACDLabs 10.04O=C(O)CC(N)C(=O)OP(=O)(O)OCC3OC(n2cnc1c(ncnc12)N)C(O)C3O
CACTVS 3.341N[C@@H](CC(O)=O)C(=O)O[P@](O)(=O)OC[C@H]1O[C@H]([C@H](O)[C@@H]1O)n2cnc3c(N)ncnc23
FormulaC14 H19 N6 O10 P
NameASPARTYL-ADENOSINE-5'-MONOPHOSPHATE
ChEMBL
DrugBankDB01895
ZINCZINC000031976613
PDB chain1g51 Chain B Residue 1831 [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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PDB1g51 Synthesis and recognition of aspartyl-adenylate by Thermus thermophilus aspartyl-tRNA synthetase.
Resolution2.4 Å
Binding residue
(original residue number in PDB)		E1177 S1199 Q1201 K1204 R1223 Q1232 F1235 Q1237 H1442 E1476 G1478 G1479 G1480 R1483 I1525 A1526 G1528 R1531
Binding residue
(residue number reindexed from 1)		E177 S199 Q201 K204 R223 Q232 F235 Q237 H442 E476 G478 G479 G480 R483 I525 A526 G528 R531
Annotation score3
Enzymatic activity
Catalytic site (original residue number in PDB) R1223 E1225 R1231 Q1232 E1476 G1479 R1531
Catalytic site (residue number reindexed from 1) R223 E225 R231 Q232 E476 G479 R531
Enzyme Commision number 6.1.1.12: aspartate--tRNA ligase.
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0003676 nucleic acid binding
GO:0004812 aminoacyl-tRNA ligase activity
GO:0004815 aspartate-tRNA ligase activity
GO:0005524 ATP binding
GO:0016874 ligase activity
Biological Process
GO:0006412 translation
GO:0006418 tRNA aminoacylation for protein translation
GO:0006422 aspartyl-tRNA aminoacylation
Cellular Component
GO:0005737 cytoplasm

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1g51, PDBe:1g51, PDBj:1g51
PDBsum1g51
PubMed7966328
UniProtP36419|SYD_THETH Aspartate--tRNA(Asp) ligase (Gene Name=aspS)

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