Structure of PDB 6gfm Chain A

Receptor sequence
>6gfmA (length=440) Species: 83333 (Escherichia coli K-12) [Search protein sequence]
LRAITHISPLGSMDMLSQLEVDMLKRTASSDLYQLFRNCSLAVLNSGSLT
DNSKELLSRFENFDINVLRRERGVKLELINPPEEAFVDGRIIRALQANLF
AVLRDILFVYGQIHNTVRFPNLNLDNSVHITNLVFSILRNARALHVGEAP
NMVVCWGGHSINENEYLYARRVGNQLGLRELNICTGCGPGAMEAPMKGAA
VGHAQQRYKDSRFIGMTEPSIIAAEPPNPLVNELIIMPDIEKRLEAFVRI
AHGIIIFPGGVGTAEELLYLLGILMNPANKDQVLPLILTGPKESADYFRV
LDEFVVHTLGENARRHYRIIIDDAAEVARQMKKSMPLVKENRRDTGDAYS
FNWSMRIAPDLQMPFEPSHENMANLKLYPDQPVEVLAADLRRAFSGIVAG
NVKEVGIRAIEEFGPYKINGDKEIMRRMDDLLQGFVAQHR
3D structure
PDB6gfm (p)ppGpp Regulates a Bacterial Nucleosidase by an Allosteric Two-Domain Switch.
ChainA
Resolution2.77 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 3.2.2.-
3.2.2.10: pyrimidine-5'-nucleotide nucleosidase.
3.2.2.4: AMP nucleosidase.
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 0O2 A R340 G343 D344 A345 Y346 R343 G346 D347 A348 Y349
Gene Ontology
Molecular Function
GO:0008714 AMP nucleosidase activity
GO:0016787 hydrolase activity
GO:0042802 identical protein binding
GO:0047405 pyrimidine-5'-nucleotide nucleosidase activity
GO:0047723 inosinate nucleosidase activity
GO:0097216 guanosine tetraphosphate binding
Biological Process
GO:0051289 protein homotetramerization
Cellular Component
GO:0005829 cytosol
GO:0032991 protein-containing complex

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:6gfm, PDBe:6gfm, PDBj:6gfm
PDBsum6gfm
PubMed31023582
UniProtP0ADR8|PPNN_ECOLI Pyrimidine/purine nucleotide 5'-monophosphate nucleosidase (Gene Name=ppnN)

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