Structure of PDB 7mtu Chain D

Receptor sequence
>7mtuD (length=349) Species: 1392 (Bacillus anthracis) [Search protein sequence]
NAMWESKFVKEGLTFDDVLLVPAKSDVLPREVSVKTVLSESLQLNIPLIS
AGMDTVTEADMAIAMARQGGLGIIHKNMSIEQQAEQVDKVKRSGGLLVGA
AVGVTADAMTRIDALVKASVDAIVLDTAHGHSQGVIDKVKEVRAKYPSLN
IIAGNVATAEATKALIEAGANVVKVGIGPGSICTTRVVAGVGVPQLTAVY
DCATEARKHGIPVIADGGIKYSGDMVKALAAGAHVVMLGSMFAGVAESPG
ETEIYQGRQFKVYRGMGSVGAMEKKLVPEGIEGRVPYKGPLADTVHQLVG
GLRAGMGYCGAQDLEFLRENAQFIRMSGAGLLESHPHHVQITKEAPNYS
3D structure
PDB7mtu Crystal Structure of the Catalytic Domain of the Inosine Monophosphate Dehydrogenase from Bacillus anthracis in the complex with IMP and the inhibitor P221
ChainD
Resolution2.34 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 ZO7 D L26 P27 A441 G444 Y445 L28 P29 A304 G307 Y308
BS02 IMP D M51 G305 S306 I307 C308 D341 G364 S365 Y388 G390 M391 G392 E416 M53 G180 S181 I182 C183 D216 G239 S240 Y263 G265 M266 G267 E279
BS03 ZO7 D T252 A253 H254 G392 E416 T127 A128 H129 G267 E279
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:7mtu, PDBe:7mtu, PDBj:7mtu
PDBsum7mtu
PubMed
UniProtA0A6L8P2U9

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