Structure of PDB 2ake Chain A

Receptor sequence
>2akeA (length=373) Species: 9606 (Homo sapiens) [Search protein sequence]
GIDYDKLIVRFGSSKIDKELINRIERATGQRPHHFLRRGIFFSHRDMNQV
LDAYENKKPFYLYTGRGPSSEAMHVGHLIPFIFTKWLQDVFNVPLVIQMT
DDEKYLWKDLTLDQAYSYAVENAKDIIACGFDINKTFIFSDLDYMGMSSG
FYKNVVKIQKHVTFNQVKGIFGFTDSDCIGKISFPAIQAAPSFSNSFPQI
FRDRTDIQCLIPCAIDQDPYFRMTRDVAPRIGYPKPALLHSTFFPALQGA
QTKMSASDPNSSIFLTDTAKQIKTKVNKHAFSGGRDTIEEHRQFGGNCDV
DVSFMYLTFFLEDDDKLEQIRKDYTSGAMLTGELKKALIEVLQPLIAEHQ
ARRKEVTDEIVKEFMTPRKLSFD
3D structure
PDB2ake Structure of human tryptophanyl-tRNA synthetase in complex with tRNA(Trp) reveals the molecular basis of tRNA recognition and specificity
ChainA
Resolution3.1 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 6.1.1.2: tryptophan--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 A S272 N373 K374 A376 F377 S378 G380 R381 D382 T383 I384 L426 T427 G428 K431 S176 N277 K278 A280 F281 S282 G284 R285 D286 T287 I288 L330 T331 G332 K335
BS02 TRP A Y159 T160 G161 R162 G163 Q194 E199 Q284 Q313 F317 Y63 T64 G65 R66 G67 Q98 E103 Q188 Q217 F221
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
PDBsum2ake
PubMed16798914
UniProtP23381|SYWC_HUMAN Tryptophan--tRNA ligase, cytoplasmic (Gene Name=WARS1)

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