7MTU

Crystal Structure of the Catalytic Domain of the Inosine Monophosphate Dehydrogenase from Bacillus anthracis in the complex with IMP and the inhibitor P221

Replaces:  5UUW

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
A	0003938	molecular_function	IMP dehydrogenase activity
A	0006164	biological_process	purine nucleotide biosynthetic process
A	0016491	molecular_function	oxidoreductase activity
B	0003824	molecular_function	catalytic activity
B	0003938	molecular_function	IMP dehydrogenase activity
B	0006164	biological_process	purine nucleotide biosynthetic process
B	0016491	molecular_function	oxidoreductase activity
C	0003824	molecular_function	catalytic activity
C	0003938	molecular_function	IMP dehydrogenase activity
C	0006164	biological_process	purine nucleotide biosynthetic process
C	0016491	molecular_function	oxidoreductase activity
D	0003824	molecular_function	catalytic activity
D	0003938	molecular_function	IMP dehydrogenase activity
D	0006164	biological_process	purine nucleotide biosynthetic process
D	0016491	molecular_function	oxidoreductase activity
E	0003824	molecular_function	catalytic activity
E	0003938	molecular_function	IMP dehydrogenase activity
E	0006164	biological_process	purine nucleotide biosynthetic process
E	0016491	molecular_function	oxidoreductase activity
F	0003824	molecular_function	catalytic activity
F	0003938	molecular_function	IMP dehydrogenase activity
F	0006164	biological_process	purine nucleotide biosynthetic process
F	0016491	molecular_function	oxidoreductase activity
G	0003824	molecular_function	catalytic activity
G	0003938	molecular_function	IMP dehydrogenase activity
G	0006164	biological_process	purine nucleotide biosynthetic process
G	0016491	molecular_function	oxidoreductase activity
H	0003824	molecular_function	catalytic activity
H	0003938	molecular_function	IMP dehydrogenase activity
H	0006164	biological_process	purine nucleotide biosynthetic process
H	0016491	molecular_function	oxidoreductase activity

Functional Information from PROSITE/UniProt

site_id	PS00487
Number of Residues	13
Details	IMP_DH_GMP_RED IMP dehydrogenase / GMP reductase signature. VKVGIGpGSICtT

Chain	Residue	Details
A	VAL298-THR310

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