Structure of PDB 3kfu Chain I Binding Site BS01
Receptor Information
>3kfu Chain I (length=444) Species:
300852
(Thermus thermophilus HB8) [
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YEAVIGLEVHLHLKTRTKMFCGCRADYFGAEPNTHTCPVCLGLPGALPVP
NRVAVEHGLRLALALGAEVPERLVFHRKNYFYPDLPKNYQISQYDLPLGR
GGSLPLGERRVRIKRLHLEEDAGKSLHLEGRTLLDLNRAGSPLIELVTEP
DLKTPEEARLFLQRIQALVQTLGISDASPEEGKLRADVNVSVRLGTKVEI
KNLNSFKSVQRALEYEIRRQTEILRRGEKVKQATMGFEEGSGKTYPMRAD
YRYFPEPDLPPVAIPRDWLEEVRRSLPELPWEKEARYRALGIKEKDAEVL
AYTPSLARFLDQALPLGLASPQALANWLLADVAGLLHERGLRLEETRLSP
EGLARLVGLFERGEVTSRVAKSLLPEVLEGQDAAAAAAAAAAAAAAAAAA
AAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA
Ligand information
>3kfu Chain K (length=74) [
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uccgcgguagcucaggguagagcagccggcuguuaaccgguaggucgcag
guucgaguccugcccgcggagcca
<<<<<<<..<<<<......>>>>.<<<<<.......>>>>>.....<<<<
<.......>>>>>>>>>>>>....
Receptor-Ligand Complex Structure
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PDB
3kfu
Crystal structure of a transfer-ribonucleoprotein particle that promotes asparagine formation.
Resolution
3.0 Å
Binding residue
(original residue number in PDB)
Y81 Y83 K125 H128 R139 R160 P180 E181 G183 R186 N208 N210 S211 F212 K213 L340 G345 H348 S378 R379 K382 X643 X646 X649
Binding residue
(residue number reindexed from 1)
Y80 Y82 K124 H127 R138 R159 P179 E180 G182 R185 N202 N204 S205 F206 K207 L329 G334 H337 S367 R368 K371 X417 X420 X423
Enzymatic activity
Enzyme Commision number
6.3.5.-
Gene Ontology
Molecular Function
GO:0003824
catalytic activity
GO:0016874
ligase activity
GO:0016884
carbon-nitrogen ligase activity, with glutamine as amido-N-donor
View graph for
Molecular Function
External links
PDB
RCSB:3kfu
,
PDBe:3kfu
,
PDBj:3kfu
PDBsum
3kfu
PubMed
20717102
UniProt
Q9LCX2
|GATB_THET8 Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B (Gene Name=gatB)
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