Structure of PDB 1il2 Chain B Binding Site BS01

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
>1il2 Chain D (length=70) [Search RNA sequence] [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
ccgugauaguuuaauggucagaaugggcgcuugucgcgugccagaucggg
guucaauuccccgucgcgga
<<<<<<..<<<<........>>>>.<<<<<.......>>>>>....<<<<
<.......>>>>>>>>>>>.
Receptor-Ligand Complex Structure
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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)		R1026 R1028 D1029 L1030 G1031 S1032 L1033 F1035 Q1046 F1048 R1064 R1078 N1082 N1084 E1093 P1109 D1111 N1113 H1114 V1115 N1116 T1117
Binding residue
(residue number reindexed from 1)		R26 R28 D29 L30 G31 S32 L33 F35 Q46 F48 R64 R78 N82 N84 E93 P109 D111 N113 H114 V115 N116 T117
Binding affinityPDBbind-CN: Kd=3uM
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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