Structure of PDB 7mtx Chain E

Receptor sequence
>7mtxE (length=352) Species: 1392 (Bacillus anthracis) [Search protein sequence]
QSNAMWESKFVKEGLTFDDVLLVPAKSDVLPREVSVKTVLSESLQLNIPL
ISAGMDTVTEADMAIAMARQGGLGIIHKNMSIEQQAEQVDKVKRSGGLLV
GAAVGVTADAMTRIDALVKASVDAIVLDTAHGHSQGVIDKVKEVRAKYPS
LNIIAGNVATAEATKALIEAGANVVKVGIGPGSICTTRVVAGVGVPQLTA
VYDCATEARKHGIPVIADGGIKYSGDMVKALAAGAHVVMLGSMFAGVAES
PGETEIYQGRQFKVYRGMGSVGAMEKKKLVPEGIEGRVPYKGPLADTVHQ
LVGGLRAGMGYCGAQDLEFLRENAQFIRMSGAGLLESHPHHVQITKEAPN
YS
3D structure
PDB7mtx Crystal Structure of the Catalytic Domain of the Inosine Monophosphate Dehydrogenase from Bacillus anthracis in the complex with IMP and the inhibitor P176
ChainE
Resolution2.44 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 IMP E M51 S306 I307 C308 D341 G342 G364 S365 Y388 G390 M391 G392 E416 M55 S183 I184 C185 D218 G219 G241 S242 Y265 G267 M268 G269 E282
BS02 ZO4 E T252 A253 H254 M391 G392 E416 T129 A130 H131 M268 G269 E282
BS03 ZO4 E P27 A441 G444 Y445 P31 A307 G310 Y311
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:7mtx, PDBe:7mtx, PDBj:7mtx
PDBsum7mtx
PubMed
UniProtA0A6L8P2U9

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