Structure of PDB 4myx Chain E

Receptor sequence
>4myxE (length=352) Species: 198094 (Bacillus anthracis str. Ames) [Search protein sequence]
QSNAMWESKFVKEGLTFDDVLLVPAKSDVLPREVSVKTVLSESLQLNIPL
ISAGMDTVTEADMAIAMARQGGLGIIHKNMSIEQQAEQVDKVKRSGGLLV
GAAVGVTADAMTRIDALVKASVDAIVLDTAHGHSQGVIDKVKEVRAKYPS
LNIIAGNVATAEATKALIEAGANVVKVGIGPGSICTTRVVAGVGVPQLTA
VYDCATEARKHGIPVIADGGIKYSGDMVKALAAGAHVVMLGSMFAGVAES
PGETEIYQGRQFKVYRGMGSVGAMEKGKLVPEGIEGRVPYKGPLADTVHQ
LVGGLRAGMGYCGAQDLEFLRENAQFIRMSGAGLLESHPHHVQITKEAPN
YS
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
ChainE
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 IMP E M51 G305 S306 I307 C308 D341 G342 L363 G364 S365 Y388 G390 M391 G392 E416 M55 G182 S183 I184 C185 D218 G219 L240 G241 S242 Y265 G267 M268 G269 E282
BS02 2F0 E M391 G392 E416 M268 G269 E282 BindingDB: Ki=1.5nM
BS03 2F0 E P27 A441 G444 Y445 P31 A307 G310 Y311 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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