Structure of PDB 4myx Chain G

Receptor sequence
>4myxG (length=356) Species: 198094 (Bacillus anthracis str. Ames) [Search protein sequence]
FQSNAMWESKFVKEGLTFDDVLLVPAKSDVLPREVSVKTVLSESLQLNIP
LISAGMDTVTEADMAIAMARQGGLGIIHKNMSIEQQAEQVDKVKRSGGLL
VGAAVGVTADAMTRIDALVKASVDAIVLDTAHGHSQGVIDKVKEVRAKYP
SLNIIAGNVATAEATKALIEAGANVVKVGIGPGSICTTRVVAGVGVPQLT
AVYDCATEARKHGIPVIADGGIKYSGDMVKALAAGAHVVMLGSMFAGVAE
SPGETEIYQGRQFKVYRGMGSVGAMEKGSKKKLVPEGIEGRVPYKGPLAD
TVHQLVGGLRAGMGYCGAQDLEFLRENAQFIRMSGAGLLESHPHHVQITK
EAPNYS
3D structure
PDB4myx Crystal Structure of the Inosine 5'-monophosphate Dehydrogenase, with a Internal Deletion of CBS Domain from Bacillus anthracis str. Ame complexed with P32
ChainG
Resolution2.701 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 2F0 G A253 M391 G392 E416 A131 M269 G270 E286 BindingDB: Ki=1.5nM
BS02 IMP G M51 S306 I307 C308 D341 G364 S365 Y388 G390 M391 G392 E416 M56 S184 I185 C186 D219 G242 S243 Y266 G268 M269 G270 E286
BS03 2F0 G G444 Y445 G314 Y315 BindingDB: Ki=1.5nM
Gene Ontology
Molecular Function
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:4myx, PDBe:4myx, PDBj:4myx
PDBsum4myx
PubMed
UniProtA0A6L8P2U9

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