Structure of PDB 2ake Chain A Binding Site BS01
Receptor Information
>2ake Chain A (length=373) Species:
9606
(Homo sapiens) [
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GIDYDKLIVRFGSSKIDKELINRIERATGQRPHHFLRRGIFFSHRDMNQV
LDAYENKKPFYLYTGRGPSSEAMHVGHLIPFIFTKWLQDVFNVPLVIQMT
DDEKYLWKDLTLDQAYSYAVENAKDIIACGFDINKTFIFSDLDYMGMSSG
FYKNVVKIQKHVTFNQVKGIFGFTDSDCIGKISFPAIQAAPSFSNSFPQI
FRDRTDIQCLIPCAIDQDPYFRMTRDVAPRIGYPKPALLHSTFFPALQGA
QTKMSASDPNSSIFLTDTAKQIKTKVNKHAFSGGRDTIEEHRQFGGNCDV
DVSFMYLTFFLEDDDKLEQIRKDYTSGAMLTGELKKALIEVLQPLIAEHQ
ARRKEVTDEIVKEFMTPRKLSFD
Ligand information
>2ake Chain B (length=72) [
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gaccucguggcgcaaugguagcgcgucugacuccagaucagaagguugcg
uguucgaaucacgucgggguca
<<<<<<<..<<<.........>>>.<<<<<.......>>>>>.....<<<
<<.......>>>>>>>>>>>>.
Receptor-Ligand Complex Structure
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PDB
2ake
Structure of human tryptophanyl-tRNA synthetase in complex with tRNA(Trp) reveals the molecular basis of tRNA recognition and specificity
Resolution
3.1 Å
Binding residue
(original residue number in PDB)
S272 N373 K374 A376 F377 S378 G380 R381 D382 T383 I384 L426 T427 G428 K431
Binding residue
(residue number reindexed from 1)
S176 N277 K278 A280 F281 S282 G284 R285 D286 T287 I288 L330 T331 G332 K335
Enzymatic activity
Enzyme Commision number
6.1.1.2
: tryptophan--tRNA ligase.
Gene Ontology
Molecular Function
GO:0000166
nucleotide binding
GO:0004812
aminoacyl-tRNA ligase activity
GO:0004830
tryptophan-tRNA ligase activity
GO:0005524
ATP binding
Biological Process
GO:0006418
tRNA aminoacylation for protein translation
GO:0006436
tryptophanyl-tRNA aminoacylation
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Molecular Function
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Biological Process
External links
PDB
RCSB:2ake
,
PDBe:2ake
,
PDBj:2ake
PDBsum
2ake
PubMed
16798914
UniProt
P23381
|SYWC_HUMAN Tryptophan--tRNA ligase, cytoplasmic (Gene Name=WARS1)
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