Structure of PDB 4myx Chain C

Receptor sequence
>4myxC (length=348) Species: 198094 (Bacillus anthracis str. Ames) [Search protein sequence]
NAMWESKFVKEGLTFDDVLLVPAKSDVLPREVSVKTVLSESLQLNIPLIS
AGMDTVTEADMAIAMARQGGLGIIHKNMSIEQQAEQVDKVKRSGGLLVGA
AVGVTADAMTRIDALVKASVDAIVLDTAHGHSQGVIDKVKEVRAKYPSLN
IIAGNVATAEATKALIEAGANVVKVGIGPGSICTTRVVAGVGVPQLTAVY
DCATEARKHGIPVIADGGIKYSGDMVKALAAGAHVVMLGSMFAGVAESPG
ETEIYQGRQFKVYRGMGSVGAMEKLVPEGIEGRVPYKGPLADTVHQLVGG
LRAGMGYCGAQDLEFLRENAQFIRMSGAGLLESHPHHVQITKEAPNYS
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
ChainC
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 C G444 Y445 G306 Y307 BindingDB: Ki=1.5nM
BS02 IMP C M51 G305 S306 I307 C308 D341 G364 S365 Y388 G390 M391 G392 E416 M53 G180 S181 I182 C183 D216 G239 S240 Y263 G265 M266 G267 E278
BS03 2F0 C A253 H254 M391 G392 E416 A128 H129 M266 G267 E278 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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