Structure of PDB 1il2 Chain B Binding Site BS02

Receptor Information
>1il2 Chain B (length=585) Species: 562 (Escherichia coli) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MRTEYCGQLRLSHVGQQVTLCGWVNRRRDLGSLIFIDMRDREGIVQVFFD
PDRADALKLASELRNEFCIQVTGTVRARDEKNINRDMATGEIEVLASSLT
IINRADVLPLDSNHVNTEEARLKYRYLDLRRPEMAQRLKTRAKITSLVRR
FMDDHGFLDIETPMLTKATPEGARDYLVPSRVHKGKFYALPQSPQLFKQL
LMMSGFDRYYQIVKCFRDEDLRADRQPEFTQIDVETSFMTAPQVREVMEA
LVRHLWLEVKGVDLGDFPVMTFAEAERRYGSDKPDLRNPMELTDVADLLK
SVEFAVFAGPANDPKGRVAALRVPGGASLTRKQIDEYGNFVKIYGAKGLA
YIKVNERAKGLEGINSPVAKFLNAEIIEDILDRTAAQDGDMIFFGADNKK
IVADAMGALRLKVGKDLGLTDESKWAPLWVIDFPMFEDDGEGGLTAMHHP
FTSPKDMTAAELKAAPENAVANAYDMVINGYEVGGGSVRIHNGDMQQTVF
GILGINEEEQREKFGFLLDALKYGTPPHAGLAFGLDRLTMLLTGTDNIRD
VIAFPKTTAAACLMTEAPSFANPTALAELSIQVVK
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 chain1il2 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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PDB1il2 The structure of an AspRS-tRNA(Asp) complex reveals a tRNA-dependent control mechanism.
Resolution2.6 Å
Binding residue
(original residue number in PDB)		E1171 S1193 K1198 R1217 R1225 Q1226 F1229 Q1231 H1448 H1449 E1482 V1483 G1484 G1485 G1486 R1489 L1531 A1532 G1534 R1537
Binding residue
(residue number reindexed from 1)		E171 S193 K198 R217 R225 Q226 F229 Q231 H448 H449 E482 V483 G484 G485 G486 R489 L531 A532 G534 R537
Annotation score3
Enzymatic activity
Catalytic site (original residue number in PDB) E1482 G1485 R1537
Catalytic site (residue number reindexed from 1) E482 G485 R537
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
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:1il2, PDBe:1il2, PDBj:1il2
PDBsum1il2
PubMed11566892
UniProtP21889|SYD_ECOLI Aspartate--tRNA ligase (Gene Name=aspS)

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