Structure of PDB 5uuv Chain D

Receptor sequence
>5uuvD (length=347) Species: 1392 (Bacillus anthracis) [Search protein sequence]
NAMWESKFVKEGLTFDDVLLVPAKSDVLPREVSVKTVLSESLQLNIPLIS
AGMDTVTEADMAIAMARQGGLGIIHKNMSIEQQAEQVDKVKRSGGLLVGA
AVGVTADAMTRIDALVKASVDAIVLDTAHGHSQGVIDKVKEVRAKYPSLN
IIAGNVATAEATKALIEAGANVVKVGIGPGSICTTRVVAGVGVPQLTAVY
DCATEARKHGIPVIADGGIKYSGDMVKALAAGAHVVMLGSMFAGVAESPG
ETEIYQGRQFKVYRGMGSVGAMEKLVPEGIEGRVPYKGPLADTVHQLVGG
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
ChainD
Resolution2.75 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 8L1 D L26 P27 G444 Y445 L28 P29 G306 Y307
BS02 IMP D M51 G305 S306 I307 C308 D341 G342 G364 S365 Y388 G390 M391 G392 E416 M53 G180 S181 I182 C183 D216 G217 G239 S240 Y263 G265 M266 G267 E278
BS03 8L1 D V229 A253 H254 S257 M391 E416 V104 A128 H129 S132 M266 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

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

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