4FGH

S. aureus dihydrofolate reductase co-crystallized with ethyl-DAP isobutenyl-dihydrophthalazine inhibitor

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	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

Functional Information from PDB Data

site_id	AC1
Number of Residues	27
Details	BINDING SITE FOR RESIDUE NAP A 201

Chain	Residue
A	VAL6
A	THR46
A	LEU62
A	THR63
A	SER64
A	HIS77
A	ILE79
A	PHE92
A	GLY93
A	GLY94
A	GLN95
A	ALA7
A	THR96
A	GLU100
A	THR121
A	0U6202
A	HOH317
A	HOH326
A	HOH335
A	HOH352
A	ILE14
A	ASN18
A	GLN19
A	LEU20
A	GLY43
A	ARG44
A	LYS45

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site_id	AC2
Number of Residues	16
Details	BINDING SITE FOR RESIDUE 0U6 A 202

Chain	Residue
A	LEU5
A	VAL6
A	ALA7
A	LEU20
A	ASP27
A	LEU28
A	VAL31
A	LYS32
A	SER49
A	LEU54
A	PRO55
A	ARG57
A	PHE92
A	THR111
A	NAP201
A	HOH340

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site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE GOL A 203

Chain	Residue
A	ARG12
A	PRO125
A	TYR126
A	GLU132

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Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	VAL13-SER35

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	5
Details	BINDING: BINDING => ECO:0000305|PubMed:19280600

Chain	Residue	Details
A	LEU5
A	ASP27
A	SER49
A	ARG57
A	PHE92

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site_id	SWS_FT_FI2
Number of Residues	6
Details	BINDING: BINDING => ECO:0000269|PubMed:19280600

Chain	Residue	Details
A	LEU62
A	GLU100
A	THR121
A	VAL6
A	ILE14
A	GLY43

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