Structure of PDB 3al0 Chain B

Receptor sequence
>3al0B (length=482) Species: 243274 (Thermotoga maritima MSB8) [Search protein sequence]
MRYRPVIGLEIHVQLSTKTKAFCSCPADVFELPPNTAICPVCTGQPGALP
VPNEEMIRFAVKTALALNCKIHKYSRFDRKNYFYPDLPKGYQISQYFYPI
ATEGFLEIDGDEGRKKVRIRRLHLEEDAGKLVHEGDSITRASYSLVDMNR
CGVPLIEIVTEPDISSPREARVFMEKLRSIVRYLGVSTGDMEKGALRCDA
NISVVDTETGRQSNRVEVKNMNSFRFVERALEYEFERIVKAMERGEDVER
ETRGWDMATKITVSMRGKEEESDYRYFPEPDIPPVVLSDEYLEEVKKELP
ELPDEKAERFMREYGLPEYDAKVLTSSKELAEFFEECVKVVNRPKDLSNW
IMTEVLRELNERNIEITESKLTPQHFADLFKLMDEGKISIKIAKEIFPEV
FETGKMPSQIVEEKGLTQINDEKLIEELVKKAMEQNPKAVQDYKSGKKKA
AGFFVGYVMRETKGKANPELTNRIIQKLLEGE
3D structure
PDB3al0 Two enzymes bound to one transfer RNA assume alternative conformations for consecutive reactions.
ChainB
Resolution3.368 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 rna B R225 Y319 N349 M352 T353 L356 R357 K391 K394 A439 D442 K449 G452 F453 V455 G456 P468 R225 Y319 N349 M352 T353 L356 R357 K391 K394 A439 D442 K449 G452 F453 V455 G456 P468
BS02 ZN B C25 C39 C42 C25 C39 C42
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:3al0, PDBe:3al0, PDBj:3al0
PDBsum3al0
PubMed20882017
UniProtQ9X100|GATB_THEMA Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B (Gene Name=gatB)

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