Structure of PDB 3fi0 Chain C

Receptor sequence
>3fi0C (length=297) Species: 1422 (Geobacillus stearothermophilus) [Search protein sequence]
MKTIFSGIQTIGNYIGALRQFVELQHEYNCYFCIVDQHAITVWQDPHELR
QNIRRLAALYLAVGIDPTQATLFIQSEVPAHAQAAWMLQCIVYIGELERM
TQVSAGLLTYPPLMAADILLYNTDIVPVGEDQKQHIELTRDLAERFNKRY
GELFTIPEARIPRIMSLVDPTKKMSKSDPNPKAYITLLDDAKTIEKKIKS
SEGTIRYGISNLLNIYSTLSGQSIEELERQYEGKGYGVFKADLAQVVIET
LRPIQERYHHWMESEELDRVLDEGAEKANRVASEMVRKMEQAMGLGR
3D structure
PDB3fi0 Independent saturation of three TrpRS subsites generates a partially assembled state similar to those observed in molecular simulations.
ChainC
Resolution2.7 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) K192 K195
Catalytic site (residue number reindexed from 1) K173 K176
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 C G7 H43 M129 D132 I133 V141 G7 H38 M114 D117 I118 V126
BS02 AMP C G17 N18 I183 K192 M193 G12 N13 I164 K173 M174
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

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:3fi0, PDBe:3fi0, PDBj:3fi0
PDBsum3fi0
PubMed19174517
UniProtP00953|SYW_GEOSE Tryptophan--tRNA ligase (Gene Name=trpS)

[Back to BioLiP]