Structure of PDB 4my8 Chain B

Receptor sequence
>4my8B (length=331) Species: 198094 (Bacillus anthracis str. Ames) [Search protein sequence]
NAMWESKFVKEGLTFDDVLLVPAKSDVLPREVSVKTVLSESLQLNIPLIS
AGMDTVTEADMAIAMARQGGLGIIHKNMSIEQQAEQVDKVKRSGGLLVGA
AVGVTADAMTRIDALVKASVDAIVLDTAHGHSQGVIDKVKEVRAKYPSLN
IIAGNVATAEATKALIEAGANVVKVGIGPGSICTTRVVAGVGVPQLTAVY
DCATEARKHGIPVIADGGIKYSGDMVKALAAGAHVVMLGSMFAGVAESPG
ETEIYQGRQFKVYRGMGSVGAMEKLVPEGIEGRVPYKGPLADTVHQLVGG
LRAGMGYCGAQDLEFLRENAQFIRMSGAGLL
3D structure
PDB4my8 Crystal Structure of the Inosine 5'-monophosphate Dehydrogenase with an Internal Deletion of the CBS Domain from Bacillus anthracis str. Ames complexed with inhibitor Q21
ChainB
Resolution2.2924 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 B M51 S306 I307 C308 D341 G364 S365 Y388 G390 M391 G392 E416 M53 S181 I182 C183 D216 G239 S240 Y263 G265 M266 G267 E278
BS02 Q21 B A253 S257 M391 M397 E416 A128 S132 M266 M272 E278 BindingDB: Ki=17nM
BS03 Q21 B S23 V25 L26 P27 A441 G444 Y445 S25 V27 L28 P29 A303 G306 Y307 BindingDB: Ki=17nM
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:4my8, PDBe:4my8, PDBj:4my8
PDBsum4my8
PubMed
UniProtA0A6L8P2U9

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