Structure of PDB 3lrt Chain A

Receptor sequence
>3lrtA (length=284) Species: 50339 (Thermoplasma volcanium) [Search protein sequence]
MKIIALRSSLKLAARIAEELKTEPVMPDERRFPDGELYLRYDEDLTGHNI
FIIGNTHSDAEVMEMILTLSAIQDYRTKSVNIIAPYYGYARQHQRYKNGE
PISSQILTEIYSSYSNSIATVDIHDEKTLSYSKVKFSDLHANDAIVRYYK
NVDVDYVVSPDDGGLARVADISAKLGKKHFFIEKKRIDDRTVEMKVPNVD
VNGKKLLIVDDIISTGGTIAKSSGLLREKGASKIYVSAVHGLFVNGSENK
ILQNADEIHVTDTVESKFSDISVYQEVCNYIRDI
3D structure
PDB3lrt The structures of Thermoplasma volcanium phosphoribosyl pyrophosphate synthetase bound to ribose-5-phosphate and ATP analogs.
ChainA
Resolution1.534 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 SO4 A S214 T215 G216 T218 S214 T215 G216 T218
BS02 SO4 A R7 S58 R7 S58
BS03 SO4 A K11 R15 K11 R15
BS04 ADP A R91 Q92 H93 Y96 R91 Q92 H93 Y96
BS05 ADP A F32 D34 E36 F32 D34 E36
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0004749 ribose phosphate diphosphokinase activity
GO:0005524 ATP binding
GO:0016301 kinase activity
GO:0046872 metal ion binding
Biological Process
GO:0006015 5-phosphoribose 1-diphosphate biosynthetic process
GO:0006164 purine nucleotide biosynthetic process
GO:0009165 nucleotide biosynthetic process
GO:0016310 phosphorylation
Cellular Component
GO:0002189 ribose phosphate diphosphokinase complex
GO:0005737 cytoplasm

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:3lrt, PDBe:3lrt, PDBj:3lrt
PDBsum3lrt
PubMed21963988
UniProtQ97CA5|KPRS_THEVO Ribose-phosphate pyrophosphokinase (Gene Name=prs)

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