Structure of PDB 3fi0 Chain K

Receptor sequence
>3fi0K (length=296) Species: 1422 (Geobacillus stearothermophilus) [Search protein sequence]
MKTIFSGIQTIGNYIGALRQFVELQHEYNCYFCIVDQHAITVWQDPHELR
QNIRRLAALYLAVGIDPTQATLFIQSEVPAHAQAAWMLQCIVYIGELERM
TVSAGLLTYPPLMAADILLYNTDIVPVGEDQKQHIELTRDLAERFNKRYG
ELFTIPEARIPKVGARIMSLVDPTKKMSKSDPNPKAYITLLDDAKTIEKK
IKSSEGTIRYGISNLLNIYSTLSGELERQYEGKGYGVFKADLAQVVIETL
RPIQERYHHWMESEELDRVLDEGAEKANRVASEMVRKMEQAMGLGR
3D structure
PDB3fi0 Independent saturation of three TrpRS subsites generates a partially assembled state similar to those observed in molecular simulations.
ChainK
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) 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 K H43 M129 D132 I133 V141 H38 M113 D116 I117 V125
BS02 AMP K G17 N18 G21 A22 I176 R182 I183 K192 M193 G12 N13 G16 A17 I160 R166 I167 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

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]