Structure of PDB 3fi0 Chain P

Receptor sequence
>3fi0P (length=295) Species: 1422 (Geobacillus stearothermophilus) [Search protein sequence]
MKTIFSGIQTIGNYIGALRQFVELQHEYNCYFCIVDQHAITVWQDPHELR
QNIRRLAALYLAVGIDPTQATLFIQSEVPAHAQAAWMLQCIVYIGELERM
TVSAGLLTYPPLMAADILLYNTDIVPVGEDQKQHIELTRDLAERFNKRYG
ELFTIPEARIPKVGARIMSLVDPTKKMSKSDPNPKAYITLLDDAKTIEKK
IKSSEGTIRYGISNLLNIYSTLSGQSIEELERQYGVFKADLAQVVIETLR
PIQERYHHWMESEELDRVLDEGAEKANRVASEMVRKMEQAMGLGR
3D structure
PDB3fi0 Independent saturation of three TrpRS subsites generates a partially assembled state similar to those observed in molecular simulations.
ChainP
Resolution2.7 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) K192 K195
Catalytic site (residue number reindexed from 1) K176 K179
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 TRP P F5 V40 H43 M129 D132 I133 Q147 F5 V35 H38 M113 D116 I117 Q131
BS02 AMP P G17 G144 K192 M193 G12 G128 K176 M177
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:3fi0, PDBe:3fi0, PDBj:3fi0
PDBsum3fi0
PubMed19174517
UniProtP00953|SYW_GEOSE Tryptophan--tRNA ligase (Gene Name=trpS)

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