Structure of PDB 3fhj Chain F

Receptor sequence
>3fhjF (length=296) Species: 1422 (Geobacillus stearothermophilus) [Search protein sequence]
MKTIFSGIQPSGVITIGNYIGALRQFVELQHEYNCYFCIVDQHAITVWQD
PHELRQNIRRLAALYLAVGIDPTQATLFIQSEVPAHAQAAWMLQCIVYIG
ELERMVSAGLLTYPPLMAADILLYNTDIVPVGEDQKQHIELTRDLAERFN
KRYFTIPEARRIMSLVDPTKKMSKSDPNPKAYITLLDDAKTIEKKIKSSE
GTIRYPGISNLLNIYSTLSGQSIEELERQYEGKGYGVFKADLAQVVIETL
RPIQERYHHWMESEELDRVLDEGAEKANRVASEMVRKMEQAMGLGR
3D structure
PDB3fhj Independent saturation of three TrpRS subsites generates a partially assembled state similar to those observed in molecular simulations.
ChainF
Resolution2.65 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) K171 K174
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 F F5 G7 H43 M129 I133 V141 F5 G7 H43 M117 I121 V129
BS02 PO4 F N18 S194 K195 N18 S173 K174
BS03 AMP F G17 N18 I183 K192 M193 G17 N18 I162 K171 M172
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:3fhj, PDBe:3fhj, PDBj:3fhj
PDBsum3fhj
PubMed19174517
UniProtP00953|SYW_GEOSE Tryptophan--tRNA ligase (Gene Name=trpS)

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