Structure of PDB 7pmz Chain D Binding Site BS03
Receptor Information
>7pmz Chain D (length=428) Species:
100226
(Streptomyces coelicolor A3(2)) [
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GVPEKFATLGLTYDDVLLLPGASAVLPNAVDTSSRISRNVRVNIPLLSAA
MDKVTESRMAISMARQGGVGVLHRNLSIEDQANQVDLVKRSESGMVANPI
TIHPDATLGEADALCAKFRISGVPVTDGAGKLLGIVTNRDMAFETDRSRQ
VREVMTPMPLVTGQVGISGVDAMELLRRHKIEKLPLVDGDGILKGLITVK
DFVKAEQYPHAAKDAKGRLLVGAAVGASPEALDRAQALAEAGVDFLVVDT
SHGHNSNALSWMSKIKSSVGIDVVGGNVATRDGAQALIDAGVDGIKVGVG
PGSICTTRVVAGIGVPQVTAIYEASLAARAAGVPLIGDGGLQYSGDIGKA
LAAGADTVMLGSLLAGCEESPGELQFINGKQFKVPYRGPLANVLHQLVGG
LRQTMGYVGAATIEEMESKGRFVRITSA
Ligand information
Ligand ID
MG
InChI
InChI=1S/Mg/q+2
InChIKey
JLVVSXFLKOJNIY-UHFFFAOYSA-N
SMILES
Software
SMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Mg+2]
CACTVS 3.341
[Mg++]
Formula
Mg
Name
MAGNESIUM ION
ChEMBL
DrugBank
DB01378
ZINC
PDB chain
7pmz Chain D Residue 603 [
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Receptor-Ligand Complex Structure
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PDB
7pmz
Diversity of mechanisms to control bacterial GTP homeostasis by the mutually exclusive binding of adenine and guanine nucleotides to IMP dehydrogenase.
Resolution
2.03 Å
Binding residue
(original residue number in PDB)
S127 E188
Binding residue
(residue number reindexed from 1)
S121 E182
Annotation score
1
Enzymatic activity
Enzyme Commision number
1.1.1.205
: IMP dehydrogenase.
Gene Ontology
Molecular Function
GO:0000166
nucleotide binding
GO:0003824
catalytic activity
GO:0003938
IMP dehydrogenase activity
GO:0005524
ATP binding
GO:0016491
oxidoreductase activity
GO:0046872
metal ion binding
Biological Process
GO:0006164
purine nucleotide biosynthetic process
GO:0006177
GMP biosynthetic process
GO:0006183
GTP biosynthetic process
View graph for
Molecular Function
View graph for
Biological Process
External links
PDB
RCSB:7pmz
,
PDBe:7pmz
,
PDBj:7pmz
PDBsum
7pmz
PubMed
35481629
UniProt
Q9L0I7
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