Structure of PDB 5urs Chain C

Receptor sequence
>5ursC (length=349) Species: 1392 (Bacillus anthracis) [Search protein sequence]
SNAMWESKFVKEGLTFDDVLLVPAKSDVLPREVSVKTVLSESLQLNIPLI
SAGMDTVTEADMAIAMARQGGLGIIHKNMSIEQQAEQVDKVKRSGGLLVG
AAVGVTADAMTRIDALVKASVDAIVLDTAHGHSQGVIDKVKEVRAKYPSL
NIIAGNVATAEATKALIEAGANVVKVGIGPGSICTTRVVAGVGVPQLTAV
YDCATEARKHGIPVIADGGIKYSGDMVKALAAGAHVVMLGSMFAGVAESP
GETEIYQGRQFKVYRGMGSVGAMEKLVPEGIEGRVPYKGPLADTVHQLVG
GLRAGMGYCGAQDLEFLRENAQFIRMSGAGLLESHPHHVQITKEAPNYS
3D structure
PDB5urs Crystal Structure of the Catalytic Domain of the Inosine Monophosphate Dehydrogenase from Bacillus anthracis in the complex with IMP and the inhibitor P178
ChainC
Resolution2.388 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 8LA C G444 Y445 G307 Y308
BS02 IMP C M51 G305 S306 I307 C308 D341 G342 G343 G364 S365 G390 M391 G392 E416 M54 G181 S182 I183 C184 D217 G218 G219 G240 S241 G266 M267 G268 E279
BS03 8LA C T252 A253 H254 S257 G259 M391 G392 M397 E416 T128 A129 H130 S133 G135 M267 G268 M273 E279
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:5urs, PDBe:5urs, PDBj:5urs
PDBsum5urs
PubMed
UniProtA0A6L8P2U9

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