Structure of PDB 1li7 Chain B

Receptor sequence
>1li7B (length=375) Species: 562 (Escherichia coli) [Search protein sequence]
MLKIFNTLTRQKEEFKPIHAGEVGMYVCGITVYDLCHIGHGRTFVAFDVV
ARYLRFLGYKLKYVRNITDIDDKIIKRESFVAMVDRMIAEMHKDFDALNI
LRPDMEPRATHHIAEIIELTEQLIAKGHAYVADNGDVMFDVPTDPTYGVL
SRQRNPMDFVLWKMSKEGEPSWPSPWGAGRPGWHIECSAMNCKQLGNHFD
IHGGGSDLMFPHHENEIAQSTCAHDGQYVNYWMHSGMVMVDREKMNFFTV
RDVLKYYDAETVRYFLMSGHYRSQLNYSEENLKQARAALERLYTALRGTD
KTVAPAGGEAFEARFIEAMDDDFNTPEAYSVLFDMAREVNRLKAEDMAAA
NAMASHLRKLSAVLGLLEQEPEAFL
3D structure
PDB1li7 Structural origins of amino acid selection without editing by cysteinyl-tRNA synthetase
ChainB
Resolution2.6 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H37 H40
Catalytic site (residue number reindexed from 1) H37 H40
Enzyme Commision number 6.1.1.16: cysteine--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 ZN B C209 H234 C187 H212
BS02 CYS B C28 G29 I30 T31 T68 W205 H234 C28 G29 I30 T31 T68 W183 H212
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0004812 aminoacyl-tRNA ligase activity
GO:0004817 cysteine-tRNA ligase activity
GO:0005524 ATP binding
GO:0008270 zinc ion binding
GO:0016874 ligase activity
GO:0046872 metal ion binding
Biological Process
GO:0006412 translation
GO:0006418 tRNA aminoacylation for protein translation
GO:0006423 cysteinyl-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:1li7, PDBe:1li7, PDBj:1li7
PDBsum1li7
PubMed12032090
UniProtP21888|SYC_ECOLI Cysteine--tRNA ligase (Gene Name=cysS)

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