Structure of PDB 7xn3 Chain A

Receptor sequence
>7xn3A (length=305) Species: 511145 (Escherichia coli str. K-12 substr. MG1655) [Search protein sequence]
DMKLFAGNATPELAQRIANRLYTSLGDAAVGRFSDGEVSVQINENVRGGD
IFIIQSTCAPTNDNLMELVVMVDALRRASAGRITAVIPYFGYARQDRRVR
SARVPITAKVVADFLSSVGVDRVLTVDLHAEQIQGFFDVPVDNVFGSPIL
LEDMLQLNLDNPIVVSPDIGGVVRARAIAKLLNDTDMAIIDKRVMHIIGD
VAGRDCVLVDDMIDTGGTLCKAAEALKERGAKRVFAYATHPIFSGNAANN
LRNSVIDEVVVCDTIPLSDEIKSLPNVRTLTLSGMLAEAIRRISNEESIS
AMFEH
3D structure
PDB7xn3 Filamentation modulates allosteric regulation of PRPS.
ChainA
Resolution2.9 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 2.7.6.1: ribose-phosphate 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 PO4 A N47 R49 N45 R47
BS02 PO4 A D224 T225 G226 T228 D214 T215 G216 T218
BS03 PO4 A S308 S310 S298 S300
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0004749 ribose phosphate diphosphokinase activity
GO:0005515 protein binding
GO:0005524 ATP binding
GO:0016301 kinase activity
GO:0042301 phosphate ion binding
GO:0042802 identical protein binding
GO:0043531 ADP binding
GO:0046872 metal ion binding
Biological Process
GO:0006015 5-phosphoribose 1-diphosphate biosynthetic process
GO:0006164 purine nucleotide biosynthetic process
GO:0009156 ribonucleoside monophosphate biosynthetic process
GO:0009165 nucleotide biosynthetic process
GO:0016310 phosphorylation
GO:0034214 protein hexamerization
GO:0044249 cellular biosynthetic process
Cellular Component
GO:0002189 ribose phosphate diphosphokinase complex
GO:0005737 cytoplasm
GO:0005829 cytosol

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:7xn3, PDBe:7xn3, PDBj:7xn3
PDBsum7xn3
PubMed35736577
UniProtP0A717|KPRS_ECOLI Ribose-phosphate pyrophosphokinase (Gene Name=prs)

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