Structure of PDB 4qm1 Chain A

Receptor sequence
>4qm1A (length=337) Species: 1392 (Bacillus anthracis) [Search protein sequence]
FQSNAMWESKFVKEGLTFDDVLLVPAKSDVLPREVSVKTVLSESLQLNIP
LISAGMDTVTEADMAIAMARQGGLGIIHKNMSIEQQAEQVDKVKRSGGLL
VGAAVGVTADAMTRIDALVKASVDAIVLDTAHGHSQGVIDKVKEVRAKYP
SLNIIAGNVATAEATKALIEAGANVVKVGIGPGSICTTRVVAGVGVPQLT
AVYDCATEARKHGIPVIADGGIKYSGDMVKALAAGAHVVMLGSMFAGVAE
SPGETEIYQGRQFKVYRGMGSVGAMEKVPEGIEGRVPYKGPLADTVHQLV
GGLRAGMGYCGAQDLEFLRENAQFIRMSGAGLLVQIT
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
ChainA
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 IMP A M51 S306 I307 C308 D341 G342 G364 S365 Y388 G390 M391 G392 E416 M56 S184 I185 C186 D219 G220 G242 S243 Y266 G268 M269 G270 E280
BS02 39H A S23 P27 G444 Y445 S28 P32 G308 Y309 BindingDB: Ki=12nM
BS03 39H A A253 S257 A131 S135 BindingDB: Ki=12nM
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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