Structure of PDB 8p4q Chain G

Receptor sequence
>8p4qG (length=389) Species: 1148 (Synechocystis sp. PCC 6803) [Search protein sequence]
GSHMNITIGRGKTARRAYGIDEIALVPGVRTLDPALADTRWKVGAIEREI
PIIASAMDGVVDSRMAVLLSELGALGVVNLEGIQTRYEDPNPILDRIASV
GKTEFVGLMQELYAEPIKPELITKRIQEIQAAGGIAAVSLTPVGASKYAS
TVAEAGADLLFIQATVVSTAHLSPSVESLDLVKLCQEMPMPVVLGNCVTY
EVSLELMRAGAAAVLVGIGPGAACTSRGVLGVGVPQPTAIADCAAARDDY
LQETGRYVPVIADGGIITGGDICKCIACGADAVMIGSPIARAAEAPGRGF
HWGMATPSPVLPRGTRINVGTTGTIREILVGPAKLDDGTHNLLGAIKTSM
GTLGAKDMKEMQQVDVVIAPSLLTEGKVYQKAQQLGMGK
3D structure
PDB8p4q GuaB3, an overlooked enzyme in cyanobacteria's toolbox that sheds light on IMP dehydrogenase evolution.
ChainG
Resolution1.88 Å
3D
structure
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Enzymatic activity
Enzyme Commision number ?
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 IMP G S52 M54 G219 A220 C222 D261 G284 G301 M302 A303 R311 S55 M57 G221 A222 C224 D263 G286 G303 M304 A305 R313
BS02 XMP G S52 M54 G219 A220 C222 S224 D261 M282 G284 H299 G301 M302 A303 S55 M57 G221 A222 C224 S226 D263 M284 G286 H301 G303 M304 A305
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0003824 catalytic activity
GO:0003938 IMP dehydrogenase activity
GO:0016491 oxidoreductase activity
Biological Process
GO:0006164 purine nucleotide biosynthetic process

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Molecular Function
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Biological Process
External links
PDB RCSB:8p4q, PDBe:8p4q, PDBj:8p4q
PDBsum8p4q
PubMed37875114
UniProtP73853

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