5SCV

Crystal Structure of Dihydrofolate Reductase from Mycobacterium tuberculosis bound to NADP and SDDC Inhibitor SDDC-889

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004146	molecular_function	dihydrofolate reductase activity
A	0005829	cellular_component	cytosol
A	0006730	biological_process	one-carbon metabolic process
A	0016491	molecular_function	oxidoreductase activity
A	0044281	biological_process	small molecule metabolic process
A	0046452	biological_process	dihydrofolate metabolic process
A	0046654	biological_process	tetrahydrofolate biosynthetic process
A	0046655	biological_process	folic acid metabolic process
A	0050661	molecular_function	NADP binding
A	0070401	molecular_function	NADP+ binding
B	0004146	molecular_function	dihydrofolate reductase activity
B	0005829	cellular_component	cytosol
B	0006730	biological_process	one-carbon metabolic process
B	0016491	molecular_function	oxidoreductase activity
B	0044281	biological_process	small molecule metabolic process
B	0046452	biological_process	dihydrofolate metabolic process
B	0046654	biological_process	tetrahydrofolate biosynthetic process
B	0046655	biological_process	folic acid metabolic process
B	0050661	molecular_function	NADP binding
B	0070401	molecular_function	NADP+ binding

Functional Information from PROSITE/UniProt

site_id	PS00075
Number of Residues	23
Details	DHFR_1 Dihydrofolate reductase (DHFR) domain signature. VIGrggdIPWrlpe.DqahFreiT

Chain	Residue	Details
A	VAL13-THR35

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	50
Details	Binding site: {}

Chain

Residue

Details

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