Structure of PDB 7pmz Chain O

Receptor sequence
>7pmzO (length=425) Species: 100226 (Streptomyces coelicolor A3(2)) [Search protein sequence]
GVPEKFATLGLTYDDVLLLPGASAVLPNAVDTSSRISRNVRVNIPLLSAA
MDKVTESRMAISMARQGGVGVLHRNLSIEDQANQVDLVKRSESGMVANPI
TIHPDATLGEADALCAKFRISGVPVTDGAGKLLIVTNRDMAFETDRSRQV
REVMTPLVTGQVGISGVDAMELLRRHKIEKLPLVDGDGILKGLITVKDFV
KAEQYPHAAKDAKGRLLVGAAVGASPEALDRAQALAEAGVDFLVVDTSHG
HNSNALSWMSKIKSSVGIDVVGGNVATRDGAQALIDAGVDGIKVGVGPGS
ICTTRVVAGIGVPQVTAIYEASLAARAAGVPLIGDGGLQYSGDIGKALAA
GADTVMLGSLLAGCEESPGELQFINGKQFKVPYRGPLANVLHQLVGGLRQ
TMGYVGAATIEEMESKGRFVRITSA
3D structure
PDB7pmz Diversity of mechanisms to control bacterial GTP homeostasis by the mutually exclusive binding of adenine and guanine nucleotides to IMP dehydrogenase.
ChainO
Resolution2.03 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 1.1.1.205: IMP dehydrogenase.
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 ATP O S127 T143 N144 R145 D146 T162 V167 I187 E188 K189 S121 T136 N137 R138 D139 T155 V158 I178 E179 K180
BS02 G4P O R71 C121 A122 R125 I126 S127 N144 E188 K206 K210 R65 C115 A116 R119 I120 S121 N137 E179 K197 K201
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

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Molecular Function
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Biological Process
External links
PDB RCSB:7pmz, PDBe:7pmz, PDBj:7pmz
PDBsum7pmz
PubMed35481629
UniProtQ9L0I7

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