Structure of PDB 5uuv Chain C

Receptor sequence
>5uuvC (length=347) Species: 1392 (Bacillus anthracis) [Search protein sequence]
AMWESKFVKEGLTFDDVLLVPAKSDVLPREVSVKTVLSESLQLNIPLISA
GMDTVTEADMAIAMARQGGLGIIHKNMSIEQQAEQVDKVKRSGGLLVGAA
VGVTADAMTRIDALVKASVDAIVLDTAHGHSQGVIDKVKEVRAKYPSLNI
IAGNVATAEATKALIEAGANVVKVGIGPGSICTTRVVAGVGVPQLTAVYD
CATEARKHGIPVIADGGIKYSGDMVKALAAGAHVVMLGSMFAGVAESPGE
TEIYQGRQFKVYRGMGSVGAMEKGLVPEGIEGRVPYKGPLADTVHQLVGG
LRAGMGYCGAQDLEFLRENAQFIRMSGAGLLESHPHHVQITKEAPNY
3D structure
PDB5uuv Crystal Structure of the Catalytic Domain of the Inosine Monophosphate Dehydrogenase from Bacillus anthracis in the complex with a product IMP and the inhibitor P182
ChainC
Resolution2.75 Å
3D
structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
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 8L1 C P27 G444 Y445 P28 G306 Y307
BS02 IMP C M51 G305 S306 I307 C308 D341 G342 G364 S365 Y388 G390 M391 G392 E416 M52 G179 S180 I181 C182 D215 G216 G238 S239 Y262 G264 M265 G266 E278
BS03 8L1 C A253 S257 M391 G392 M397 E416 A127 S131 M265 G266 M271 E278
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

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:5uuv, PDBe:5uuv, PDBj:5uuv
PDBsum5uuv
PubMed
UniProtA0A6L8P2U9

[Back to BioLiP]