Structure of PDB 4qm1 Chain C

Receptor sequence
>4qm1C (length=332) Species: 1392 (Bacillus anthracis) [Search protein sequence]
SNAMWESKFVKEGLTFDDVLLVPAKSDVLPREVSVKTVLSESLQLNIPLI
SAGMDTVTEADMAIAMARQGGLGIIHKNMSIEQQAEQVDKVKRSGGLLVG
AAVGVTADAMTRIDALVKASVDAIVLDTAHGHSQGVIDKVKEVRAKYPSL
NIIAGNVATAEATKALIEAGANVVKVGIGPGSICTTRVVAGVGVPQLTAV
YDCATEARKHGIPVIADGGIKYSGDMVKALAAGAHVVMLGSMFAGVAESP
GETEIYQGRQFKVYRGMGSVGAMVPEGIEGRVPYKGPLADTVHQLVGGLR
AGMGYCGAQDLEFLRENAQFIRMSGAGLLVQI
3D structure
PDB4qm1 Crystal Structure of the Inosine 5'-monophosphate Dehydrogenase with an Internal Deletion of the CBS Domain from Bacillus anthracis str. Ames complexed with inhibitor D67
ChainC
Resolution2.7964 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 39H C S23 P27 G444 Y445 S26 P30 G304 Y305 BindingDB: Ki=12nM
BS02 39H C A253 M391 G392 E416 A129 M267 G268 E276 BindingDB: Ki=12nM
BS03 IMP C M51 S306 I307 C308 D341 G364 S365 Y388 G390 M391 G392 E416 G417 M54 S182 I183 C184 D217 G240 S241 Y264 G266 M267 G268 E276 G277
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:4qm1, PDBe:4qm1, PDBj:4qm1
PDBsum4qm1
PubMed
UniProtA0A6L8P2U9

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