Structure of PDB 3al0 Chain B Binding Site BS01

Receptor Information
>3al0 Chain B (length=482) Species: 243274 (Thermotoga maritima MSB8) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MRYRPVIGLEIHVQLSTKTKAFCSCPADVFELPPNTAICPVCTGQPGALP
VPNEEMIRFAVKTALALNCKIHKYSRFDRKNYFYPDLPKGYQISQYFYPI
ATEGFLEIDGDEGRKKVRIRRLHLEEDAGKLVHEGDSITRASYSLVDMNR
CGVPLIEIVTEPDISSPREARVFMEKLRSIVRYLGVSTGDMEKGALRCDA
NISVVDTETGRQSNRVEVKNMNSFRFVERALEYEFERIVKAMERGEDVER
ETRGWDMATKITVSMRGKEEESDYRYFPEPDIPPVVLSDEYLEEVKKELP
ELPDEKAERFMREYGLPEYDAKVLTSSKELAEFFEECVKVVNRPKDLSNW
IMTEVLRELNERNIEITESKLTPQHFADLFKLMDEGKISIKIAKEIFPEV
FETGKMPSQIVEEKGLTQINDEKLIEELVKKAMEQNPKAVQDYKSGKKKA
AGFFVGYVMRETKGKANPELTNRIIQKLLEGE
Ligand information
>3al0 Chain E (length=74) [Search RNA sequence] [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
ugggaggucgucuaacgguaggacggcggacucuggauccgcugguggag
guucgaguccuccccucccagcca
<<<<<<<..<<<<.......>>>><<<<<<.......>>>>>>...<<<<
<.......>>>>>>>>>>>>....
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB3al0 Two enzymes bound to one transfer RNA assume alternative conformations for consecutive reactions.
Resolution3.368 Å
Binding residue
(original residue number in PDB)		R225 Y319 N349 M352 T353 L356 R357 K391 K394 A439 D442 K449 G452 F453 V455 G456 P468
Binding residue
(residue number reindexed from 1)		R225 Y319 N349 M352 T353 L356 R357 K391 K394 A439 D442 K449 G452 F453 V455 G456 P468
Enzymatic activity
Enzyme Commision number 6.3.5.-
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

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:3al0, PDBe:3al0, PDBj:3al0
PDBsum3al0
PubMed20882017
UniProtQ9X100|GATB_THEMA Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B (Gene Name=gatB)

[Back to BioLiP]