Structure of PDB 4my9 Chain D

Receptor sequence
>4my9D (length=347) Species: 198094 (Bacillus anthracis str. Ames) [Search protein sequence]
NAMWESKFVKEGLTFDDVLLVPAKSDVLPREVSVKTVLSESLQLNIPLIS
AGMDTVTEADMAIAMARQGGLGIIHKNMSIEQQAEQVDKVKRSGGLLVGA
AVGVTADAMTRIDALVKASVDAIVLDTAHGHSQGVIDKVKEVRAKYPSLN
IIAGNVATAEATKALIEAGANVVKVGIGPGSICTTRVVAGVGVPQLTAVY
DCATEARKHGIPVIADGGIKYSGDMVKALAAGAHVVMLGSMFAGVAESPG
ETEIYQGRQFKVYRGMGSVGAMELVPEGIEGRVPYKGPLADTVHQLVGGL
RAGMGYCGAQDLEFLRENAQFIRMSGAGLLESHPHHVQITKEAPNYS
3D structure
PDB4my9 Crystal Structure of the Inosine 5'-monophosphate Dehydrogenase with an Internal Deletion of the CBS Domain from Bacillus anthracis str. Ames complexed with inhibitor C91
ChainD
Resolution2.5893 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 C91 D P27 A441 G444 Y445 P29 A302 G305 Y306 BindingDB: Ki=44nM
BS02 IMP D M51 G305 S306 I307 C308 D341 G364 Y388 G390 M391 G392 E416 M53 G180 S181 I182 C183 D216 G239 Y263 G265 M266 G267 E277
BS03 C91 D A253 M397 E416 A128 M272 E277 BindingDB: Ki=44nM
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:4my9, PDBe:4my9, PDBj:4my9
PDBsum4my9
PubMed
UniProtA0A6L8P2U9

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