Structure of PDB 5l3p Chain z

Receptor sequence
>5l3pz (length=545) Species: 562 (Escherichia coli) [Search protein sequence]
EFDPEKWIASLGITSQKSCECLAETWAYCLQQTQGHPDASLLLWRGVEMV
EILSTLSMDIDTLRAALLFPLADANVVSEDVLRESVGKSVVNLIHGVRDM
AAIRQDNVRRMLLAMVDDFRCVVIKLAERIAHLREDERVLAAKECTNIYA
PLANRLGIGQLKWELEDYCFRYLHPTEYKRIAKLLHERRLDREHYIEEFV
GHLRAEMKAEGVKAEVYGRPKHIYSIWRKMQKKNLAFDELFDVRAVRIVA
ERLQDCYAALGIVHTHYRHLPDEFDDYVANPKPNGYQSIHTVVLGPGGKT
VEIQIRTKQMHEDAELGDRIAWLRKLVFDDRVYVFTPKGDVVDLPAGSTP
LDFAYHIHSDVGHRCIGAKIGGRIVPFTYQLQMGDQIEIITQAAAAAAAA
AAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA
AAAAAAAAAAAAAAAAAAGYSLVVRVVANDRSGLLRDITTILANEKVNVL
GVASRSDTKQQLATIDMTIEIYNLQVLGRVLGKLNQVPDVIDARR
3D structure
PDB5l3p The stringent factor RelA adopts an open conformation on the ribosome to stimulate ppGpp synthesis.
Chainz
Resolution3.7 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 2.7.6.5: GTP diphosphokinase.
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 z I440 I448 I366 I374
BS02 rna z X514 X526 X535 X537 X538 X541 X420 X432 X441 X443 X444 X447
Gene Ontology
Biological Process
GO:0015969 guanosine tetraphosphate metabolic process

View graph for
Biological Process
External links
PDB RCSB:5l3p, PDBe:5l3p, PDBj:5l3p
PDBsum5l3p
PubMed27226493
UniProtP0AG20|RELA_ECOLI GTP pyrophosphokinase (Gene Name=relA)

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