1VIE

STRUCTURE OF DIHYDROFOLATE REDUCTASE

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004146	molecular_function	dihydrofolate reductase activity
A	0009410	biological_process	response to xenobiotic stimulus

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	7
Details	Binding site: {"evidences":[{"source":"PubMed","id":"17473013","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18052202","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2P4T","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2RK1","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2RK2","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	1
Details	Binding site: {"evidences":[{"source":"PubMed","id":"18052202","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2RK1","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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Catalytic Information from CSA

site_id	CSA1
Number of Residues	4
Details	a catalytic site defined by CSA, PubMed 15812782, 11560482

Chain	Residue	Details
A	ILE68
A	LYS32
A	TYR69
A	GLN67

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site_id	MCSA1
Number of Residues	4
Details	M-CSA 752

Chain	Residue	Details
A	LYS32	electrostatic stabiliser
A	GLN67	electrostatic stabiliser
A	ILE68	electrostatic stabiliser
A	TYR69	electrostatic stabiliser

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