Structure of PDB 1i6k Chain A

Receptor sequence
>1i6kA (length=326) Species: 1422 (Geobacillus stearothermophilus) [Search protein sequence]
MKTIFSGIQPSGVITIGNYIGALRQFVELQHEYNCYFCIVDQHAITVWQD
PHELRQNIRRLAALYLAVGIDPTQATLFIQSEVPAHAQAAWMLQCIVYIG
ELERMTQFKEKSAGKEAVSAGLLTYPPLMAADILLYNTDIVPVGEDQKQH
IELTRDLAERFNKRYGELFTIPEARIPKVGARIMSLVDPTKKMSKSDPNP
KAYITLLDDAKTIEKKIKSAVTDSEGTIRYDKEAKPGISNLLNIYSTLSG
QSIEELERQYEGKGYGVFKADLAQVVIETLRPIQERYHHWMESEELDRVL
DEGAEKANRVASEMVRKMEQAMGLGR
3D structure
PDB1i6k High-resolution experimental phases for tryptophanyl-tRNA synthetase (TrpRS) complexed with tryptophanyl-5'AMP.
ChainA
Resolution1.72 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) K111 K192 K195
Catalytic site (residue number reindexed from 1) K111 K192 K195
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 A F5 S6 G7 I8 Q9 G17 N18 G21 A22 V40 H43 Y125 M129 D132 I133 V141 V143 G144 D146 Q147 A181 R182 I183 K192 F5 S6 G7 I8 Q9 G17 N18 G21 A22 V40 H43 Y125 M129 D132 I133 V141 V143 G144 D146 Q147 A181 R182 I183 K192
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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Cellular Component
External links
PDB RCSB:1i6k, PDBe:1i6k, PDBj:1i6k
PDBsum1i6k
PubMed11679724
UniProtP00953|SYW_GEOSE Tryptophan--tRNA ligase (Gene Name=trpS)

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