Structure of PDB 3ip4 Chain B

Receptor sequence
>3ip4B (length=482) Species: 158878 (Staphylococcus aureus subsp. aureus Mu50) [Search protein sequence]
MHFETVIGLEVHVELKTDSKMFSPSPAHFGAEPNSNTNVIDLAYPGVLPV
VNKRAVDWAMRAAMALNMEIATESKFDRKNYFYPDNPKAYQISQFDQPIG
ENGYIDIEVDGETKRIGITRLHMEEDAGKSTHKGEYSLVDLNRQGTPLIE
IVSEPDIRSPKEAYAYLEKLRSIIQYTGVSDVKMEEGSLRCDANISLRPY
GQEKFGTKAELKNLNSFNYVRKGLEYEEKRQEEELLNGGEIGQETRRFDE
STGKTILMRVKEGSDDYRYFPEPDIVPLYIDDAWKERVRQTIPELPDERK
AKYVNELGLPAYDAHVLTLTKEMSDFFESTIEHGADVKLTSNWLMGGVNE
YLNKNQVELLDTKLTPENLAGMIKLIEDGTMSSKIAKKVFPELAAKGGNA
KQIMEDNGLVQISDEATLLKFVNEALDNNEQSVEDYKNGKGKAMGFLVGQ
IMKASKGQANPQLVNQLLKQELDKRLEHHHHH
3D structure
PDB3ip4 Two distinct regions in Staphylococcus aureus GatCAB guarantee accurate tRNA recognition
ChainB
Resolution1.9 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 6.3.5.-
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 MG B H12 E124 E150 H12 E124 E150
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0005524 ATP binding
GO:0016874 ligase activity
GO:0016884 carbon-nitrogen ligase activity, with glutamine as amido-N-donor
GO:0050566 asparaginyl-tRNA synthase (glutamine-hydrolyzing) activity
GO:0050567 glutaminyl-tRNA synthase (glutamine-hydrolyzing) activity
Biological Process
GO:0006412 translation
GO:0070681 glutaminyl-tRNAGln biosynthesis via transamidation

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Molecular Function
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Biological Process
External links
PDB RCSB:3ip4, PDBe:3ip4, PDBj:3ip4
PDBsum3ip4
PubMed19906721
UniProtP64201|GATB_STAAM Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B (Gene Name=gatB)

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