Structure of PDB 1vj7 Chain B

Receptor sequence
>1vj7B (length=310) Species: 119602 (Streptococcus dysgalactiae subsp. equisimilis) [Search protein sequence]
INLTGEEVVALAAKYMNETDAAFVKKALDYATAAHFYQVRKSGEPYIVHP
IQVAGILADLHLDAVTVACGFLHDVVEDTDITLDNIEFDFGKDVRDIVDG
VTKLGKVESKDIRVILVKLADRLHNMRTLKHLRKDKQERISRETMEIYAP
LAHRLGISRIKWELEDLAFRYLNETEFYKISHMMNEKLVDDIVTKIKSYT
TEQGLFGDVYGRPKHIYSIYRKMRIFDLIAIRCVMETQSDVYAMVGYIHE
LWRPMPGRFKDYIAAPKANGYQSIHTTVYGPKGPIEIQIRTKEMHQVAEY
GVAWIKELVE
3D structure
PDB1vj7 Conformational antagonism between opposing active sites in a bifunctional RelA/SpoT homolog modulates (p)ppGpp metabolism during the stringent response.
ChainB
Resolution2.1 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 2.7.6.5: GTP diphosphokinase.
3.1.7.2: guanosine-3',5'-bis(diphosphate) 3'-diphosphatase.
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 MN B H53 H77 D78 D144 H49 H73 D74 D121
BS02 GDP B S181 W185 R241 Y299 K304 N306 Y308 H312 Q325 A335 S158 W162 R212 Y262 K267 N269 Y271 H275 Q288 A298
BS03 GPX B R44 K45 S46 N148 T151 L155 K159 R40 K41 S42 N125 T128 L132 K136
Gene Ontology
Biological Process
GO:0015969 guanosine tetraphosphate metabolic process

View graph for
Biological Process
External links
PDB RCSB:1vj7, PDBe:1vj7, PDBj:1vj7
PDBsum1vj7
PubMed15066282
UniProtQ54089|RELA_STREQ Bifunctional (p)ppGpp synthase/hydrolase RelA (Gene Name=relA)

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