Structure of PDB 5urs Chain E

Receptor sequence

>5ursE (length=350) Species: 1392 (Bacillus anthracis)

FQSNAMWESKFVKEGLTFDDVLLVPAKSDVLPREVSVKTVLSESLQLNIP
LISAGMDTVTEADMAIAMARQGGLGIIHKNMSIEQQAEQVDKVKRSGGLL
VGAAVGVTADAMTRIDALVKASVDAIVLDTAHGHSQGVIDKVKEVRAKYP
SLNIIAGNVATAEATKALIEAGANVVKVGIGPGSICTTRVVAGVGVPQLT
AVYDCATEARKHGIPVIADGGIKYSGDMVKALAAGAHVVMLGSMFAGVAE
SPGETEIYQGRQFKVYRGMGSVGAMEKVPEGIEGRVPYKGPLADTVHQLV
GGLRAGMGYCGAQDLEFLRENAQFIRMSGAGLLESHPHHVQITKEAPNYS

3D structure

• PDB: 5urs Crystal Structure of the Catalytic Domain of the Inosine Monophosphate Dehydrogenase from Bacillus anthracis in the complex with IMP and the inhibitor P178
• Chain: E
• Resolution: 2.388 Å

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	E	M51 G305 S306 I307 C308 D341 G342 G343 G364 S365 Y388 G390 M391 G392 E416	M56 G183 S184 I185 C186 D219 G220 G221 G242 S243 Y266 G268 M269 G270 E280
BS02	8LA	E	T252 A253 H254 S257 G259 V260 M391 G392 M397 E416	T130 A131 H132 S135 G137 V138 M269 G270 M275 E280
BS03	8LA	E	P27 G444 Y445	P32 G308 Y309

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

External links

• PDB: RCSB:5urs, PDBe:5urs, PDBj:5urs
• PDBsum: 5urs
• UniProt: A0A6L8P2U9