Structure of PDB 3lrt Chain A Binding Site BS03

Receptor Information

>3lrt Chain A (length=284) Species: 50339 (Thermoplasma volcanium)

MKIIALRSSLKLAARIAEELKTEPVMPDERRFPDGELYLRYDEDLTGHNI
FIIGNTHSDAEVMEMILTLSAIQDYRTKSVNIIAPYYGYARQHQRYKNGE
PISSQILTEIYSSYSNSIATVDIHDEKTLSYSKVKFSDLHANDAIVRYYK
NVDVDYVVSPDDGGLARVADISAKLGKKHFFIEKKRIDDRTVEMKVPNVD
VNGKKLLIVDDIISTGGTIAKSSGLLREKGASKIYVSAVHGLFVNGSENK
ILQNADEIHVTDTVESKFSDISVYQEVCNYIRDI

Ligand information

• Ligand ID: SO4
• InChI: InChI=1S/H2O4S/c1-5(2,3)4/h(H2,1,2,3,4)/p-2
• InChIKey: QAOWNCQODCNURD-UHFFFAOYSA-L
• SMILES:
  OpenEye OEToolkits 1.5.0: [O-]S(=O)(=O)[O-]
  CACTVS 3.341: [O-][S]([O-])(=O)=O
  ACDLabs 10.04: [O-]S([O-])(=O)=O
• Formula: O4 S
• Name: SULFATE ION
• DrugBank: DB14546
• PDB chain: 3lrt Chain A Residue 289

Receptor-Ligand Complex Structure

Structure summary

• PDB: 3lrt The structures of Thermoplasma volcanium phosphoribosyl pyrophosphate synthetase bound to ribose-5-phosphate and ATP analogs.
• Resolution: 1.534 Å
• Binding residue (original residue number in PDB): K11 R15
• Binding residue (residue number reindexed from 1): K11 R15
• Annotation score: 1

Enzymatic activity

• Enzyme Commision number: 2.7.6.1: ribose-phosphate diphosphokinase.

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

External links

• PDB: RCSB:3lrt, PDBe:3lrt, PDBj:3lrt
• PDBsum: 3lrt
• PubMed: 21963988
• UniProt: Q97CA5|KPRS_THEVO Ribose-phosphate pyrophosphokinase (Gene Name=prs)