Structure of PDB 1il2 Chain B

Receptor sequence

>1il2B (length=585) Species: 562 (Escherichia coli) [Search protein sequence]

MRTEYCGQLRLSHVGQQVTLCGWVNRRRDLGSLIFIDMRDREGIVQVFFD
PDRADALKLASELRNEFCIQVTGTVRARDEKNINRDMATGEIEVLASSLT
IINRADVLPLDSNHVNTEEARLKYRYLDLRRPEMAQRLKTRAKITSLVRR
FMDDHGFLDIETPMLTKATPEGARDYLVPSRVHKGKFYALPQSPQLFKQL
LMMSGFDRYYQIVKCFRDEDLRADRQPEFTQIDVETSFMTAPQVREVMEA
LVRHLWLEVKGVDLGDFPVMTFAEAERRYGSDKPDLRNPMELTDVADLLK
SVEFAVFAGPANDPKGRVAALRVPGGASLTRKQIDEYGNFVKIYGAKGLA
YIKVNERAKGLEGINSPVAKFLNAEIIEDILDRTAAQDGDMIFFGADNKK
IVADAMGALRLKVGKDLGLTDESKWAPLWVIDFPMFEDDGEGGLTAMHHP
FTSPKDMTAAELKAAPENAVANAYDMVINGYEVGGGSVRIHNGDMQQTVF
GILGINEEEQREKFGFLLDALKYGTPPHAGLAFGLDRLTMLLTGTDNIRD
VIAFPKTTAAACLMTEAPSFANPTALAELSIQVVK

3D structure

PDB

1il2 The structure of an AspRS-tRNA(Asp) complex reveals a tRNA-dependent control mechanism.

Chain

Resolution

2.6 Å

3D
structure

Catalytic site residues are labeled in the structure
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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.

Interaction with ligand

Site #	Ligand	Ligand chain	Binding residues on receptor (original residue number in PDB)	Binding residues on receptor (residue number reindexed from 1)	Binding affinity
BS01	rna	B	R1026 R1028 D1029 L1030 G1031 S1032 L1033 F1035 Q1046 F1048 R1064 R1078 N1082 N1084 E1093 P1109 D1111 N1113 H1114 V1115 N1116 T1117	R26 R28 D29 L30 G31 S32 L33 F35 Q46 F48 R64 R78 N82 N84 E93 P109 D111 N113 H114 V115 N116 T117	PDBbind-CN: Kd=3uM
BS02	AMO	B	E1171 S1193 K1198 R1217 R1225 Q1226 F1229 Q1231 H1448 H1449 E1482 V1483 G1484 G1485 G1486 R1489 L1531 A1532 G1534 R1537	E171 S193 K198 R217 R225 Q226 F229 Q231 H448 H449 E482 V483 G484 G485 G486 R489 L531 A532 G534 R537

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
PDBsum	1il2
PubMed	11566892
UniProt	P21889\|SYD_ECOLI Aspartate--tRNA ligase (Gene Name=aspS)

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