Structure of PDB 5urs Chain H

Receptor sequence

>5ursH (length=348) Species: 1392 (Bacillus anthracis)

NAMWESKFVKEGLTFDDVLLVPAKSDVLPREVSVKTVLSESLQLNIPLIS
AGMDTVTEADMAIAMARQGGLGIIHKNMSIEQQAEQVDKVKRSGGLLVGA
AVGVTADAMTRIDALVKASVDAIVLDTAHGHSQGVIDKVKEVRAKYPSLN
IIAGNVATAEATKALIEAGANVVKVGIGPGSICTTRVVAGVGVPQLTAVY
DCATEARKHGIPVIADGGIKYSGDMVKALAAGAHVVMLGSMFAGVAESPG
ETEIYQGRQFKVYRGMGSVGAMEKLVPEGIEGRVPYKGPLADTVHQLVGG
LRAGMGYCGAQDLEFLRENAQFIRMSGAGLLESHPHHVQITKEAPNYS

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: H
• 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	8LA	H	L26 P27 G444 Y445	L28 P29 G306 Y307
BS02	IMP	H	M51 G305 S306 I307 C308 D341 L363 G364 S365 Y388 G390 M391 G392 E416	M53 G180 S181 I182 C183 D216 L238 G239 S240 Y263 G265 M266 G267 E278
BS03	8LA	H	V229 T252 A253 H254 S257 G259 M391 G392 E416	V104 T127 A128 H129 S132 G134 M266 G267 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

External links

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