Structure of PDB 4mya Chain A

Receptor sequence
>4myaA (length=349) Species: 198094 (Bacillus anthracis str. Ames) [Search protein sequence]
NAMWESKFVKEGLTFDDVLLVPAKSDVLPREVSVKTVLSESLQLNIPLIS
AGMDTVTEADMAIAMARQGGLGIIHKNMSIEQQAEQVDKVKRSGGLLVGA
AVGVTADAMTRIDALVKASVDAIVLDTAHGHSQGVIDKVKEVRAKYPSLN
IIAGNVATAEATKALIEAGANVVKVGIGPGSICTTRVVAGVGVPQLTAVY
DCATEARKHGIPVIADGGIKYSGDMVKALAAGAHVVMLGSMFAGVAESPG
ETEIYQGRQFKVYRGMGSVGAMEKKKLVPEGIEGRVPYKGPLADTVHQLV
GGLRAGMGYCGAQDLEFLRENAQFIRMSGAGLLESHPHHVQITKEAPNY
3D structure
PDB4mya Crystal Structure of the Inosine 5'-monophosphate Dehydrogenase with an Internal Deletion of the CBS Domain from Bacillus anthracis str. Ames complexed with inhibitor A110
ChainA
Resolution1.8997 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 A M51 G305 S306 I307 C308 D341 G343 G364 S365 Y388 G390 M391 G392 E416 M53 G180 S181 I182 C183 D216 G218 G239 S240 Y263 G265 M266 G267 E280
BS02 2EY A A253 H254 M391 G392 M397 L413 E416 A128 H129 M266 G267 M272 L277 E280
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:4mya, PDBe:4mya, PDBj:4mya
PDBsum4mya
PubMed
UniProtA0A6L8P2U9

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