Structure of PDB 3jxe Chain B

Receptor sequence
>3jxeB (length=363) Species: 53953 (Pyrococcus horikoshii) [Search protein sequence]
MVEEFKVTPWEVEGVVDYDKLIKHFGTSPLTEDLLEKTAELTKSELPIFF
RRKFFFSHRDYDLILKDYEEGRGFFLYTGRGPSGPMHIGHIIPFFATKWL
QEKFGVNLYIQITDDEKFLFKENLTFDDTKRWAYDNILDIIAVGFDPDKT
FIFQNSEFTKIYEMAIPIAKKINFSMAKAVFGFTEQSKIGMIFFPAIQIA
PTFFERKRCLIPAAIDQDPYWRLQRDFAESLGYYKTAALHSKFVPSLTSL
SGKMSASKPETAIYLTDSPEDVEKKVWKFTLKCVVFKWLEIFFEEDDKKL
KERYYACKNGELTCGECKRYLISKIQEFLKEHQRRRKKAEKLVEKFKYTG
KLAQEMWNEAIPE
3D structure
PDB3jxe Crystal structure of P. horikoshii tryptophanyl-tRNA synthetase and structure-based phylogenetic analysis suggest an archaeal origin of tryptophanyl-tRNA synthetase
ChainB
Resolution3.0 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 TYM B Y77 T78 G79 R80 G81 G89 H90 P93 Q111 E116 K117 Q198 A213 A214 Q217 W221 F243 V244 K253 Y77 T78 G79 R80 G81 G89 H90 P93 Q111 E116 K117 Q198 A213 A214 Q217 W221 F243 V244 K253
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:0006412 translation
GO:0006418 tRNA aminoacylation for protein translation
GO:0006436 tryptophanyl-tRNA aminoacylation
Cellular Component
GO:0005737 cytoplasm

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:3jxe, PDBe:3jxe, PDBj:3jxe
PDBsum3jxe
PubMed
UniProtO59584|SYW_PYRHO Tryptophan--tRNA ligase (Gene Name=trpS)

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