Structure of PDB 5urs Chain D

Receptor sequence
>5ursD (length=350) Species: 1392 (Bacillus anthracis) [Search protein sequence]
FQSNAMWESKFVKEGLTFDDVLLVPAKSDVLPREVSVKTVLSESLQLNIP
LISAGMDTVTEADMAIAMARQGGLGIIHKNMSIEQQAEQVDKVKRSGGLL
VGAAVGVTADAMTRIDALVKASVDAIVLDTAHGHSQGVIDKVKEVRAKYP
SLNIIAGNVATAEATKALIEAGANVVKVGIGPGSICTTRVVAGVGVPQLT
AVYDCATEARKHGIPVIADGGIKYSGDMVKALAAGAHVVMLGSMFAGVAE
SPGETEIYQGRQFKVYRGMGSVGAMELVPEGIEGRVPYKGPLADTVHQLV
GGLRAGMGYCGAQDLEFLRENAQFIRMSGAGLLESHPHHVQITKEAPNYS
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
ChainD
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 D L26 G444 Y445 L31 G308 Y309
BS02 IMP D M51 G305 S306 I307 C308 D341 G342 G364 S365 Y388 G390 M391 G392 E416 M56 G183 S184 I185 C186 D219 G220 G242 S243 Y266 G268 M269 G270 E280
BS03 8LA D A253 H254 S257 G259 M391 G392 E416 A131 H132 S135 G137 M269 G270 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:5urs, PDBe:5urs, PDBj:5urs
PDBsum5urs
PubMed
UniProtA0A6L8P2U9

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