Structure of PDB 1ibs Chain A

Receptor sequence
>1ibsA (length=297) Species: 1423 (Bacillus subtilis) [Search protein sequence]
NLKIFSLNSNPELAKEIADIVGVQLGKCSVTRFSDGEVQINIEESIRGCD
CYIIQSTSDPVNEHIMELLIMVDALKRASAKTINIVIPYYGYARQDRKSR
EPITAKLFANLLETAGATRVIALDLHAPQIQGFFDIPIDHLMGVPILGEY
FEGKNLEDIVIVSPDHGGVTRARKLADRLKAPIAIIDKRMNIVGNIEGKT
AILIDDIIDTAGTITLAANALVENGAKEVYACCTHPVLSGPAVERINNST
IKELVVTNSIKLPEEKKIERFKQLSVGPLLAEAIIRVHEQQSVSYLF
3D structure
PDB1ibs Binding of cations in Bacillus subtilis phosphoribosyldiphosphate synthetase and their role in catalysis.
ChainA
Resolution2.8 Å
3D
structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
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 D227 T228 A229 T231 D209 T210 A211 T213
BS02 ABM A R101 Q102 R104 H135 R94 Q95 R97 H126
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:0009156 ribonucleoside monophosphate biosynthetic process
GO:0009165 nucleotide biosynthetic process
GO:0016310 phosphorylation
GO:0044249 cellular biosynthetic process
Cellular Component
GO:0002189 ribose phosphate diphosphokinase complex
GO:0005737 cytoplasm

View graph for
Molecular Function

View graph for
Biological Process

View graph for
Cellular Component
External links
PDB RCSB:1ibs, PDBe:1ibs, PDBj:1ibs
PDBsum1ibs
PubMed11790837
UniProtP14193|KPRS_BACSU Ribose-phosphate pyrophosphokinase (Gene Name=prs)

[Back to BioLiP]