6DFR

CRYSTAL STRUCTURES OF ESCHERICHIA COLI DIHYDROFOLATE REDUCTASE. THE NADP+ HOLOENZYME AND THE FOLATE(DOT)NADP+ TERNARY COMPLEX. SUBSTRATE BINDING AND A MODEL FOR THE TRANSITION STATE

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004146	molecular_function	dihydrofolate reductase activity
A	0005515	molecular_function	protein binding
A	0005542	molecular_function	folic acid binding
A	0005829	cellular_component	cytosol
A	0006545	biological_process	glycine biosynthetic process
A	0006730	biological_process	one-carbon metabolic process
A	0009410	biological_process	response to xenobiotic stimulus
A	0016491	molecular_function	oxidoreductase activity
A	0031427	biological_process	response to methotrexate
A	0046452	biological_process	dihydrofolate metabolic process
A	0046654	biological_process	tetrahydrofolate biosynthetic process
A	0046655	biological_process	folic acid metabolic process
A	0046677	biological_process	response to antibiotic
A	0050661	molecular_function	NADP binding
A	0051870	molecular_function	methotrexate binding
A	0051871	molecular_function	dihydrofolic acid binding
A	0070401	molecular_function	NADP+ binding
A	0070402	molecular_function	NADPH binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	1
Details	BINDING SITE FOR RESIDUE CA A 350

Chain	Residue
A	ILE94

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site_id	AC2
Number of Residues	17
Details	BINDING SITE FOR RESIDUE NAP A 164

Chain	Residue
A	LYS76
A	GLY96
A	GLY97
A	ARG98
A	VAL99
A	GLN102
A	THR123
A	HOH248
A	HOH381
A	ILE14
A	GLY43
A	ARG44
A	HIS45
A	THR46
A	LEU62
A	SER63
A	SER64

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Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	VAL13-THR35

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	5
Details	BINDING: BINDING => ECO:0000305|PubMed:9012674

Chain	Residue	Details
A	ILE5
A	ASP27
A	ARG52
A	ARG57
A	THR113

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site_id	SWS_FT_FI2
Number of Residues	6
Details	BINDING: BINDING => ECO:0000269|PubMed:19374017

Chain	Residue	Details
A	ALA7
A	VAL13
A	HIS45
A	SER63
A	LYS76
A	GLY95

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