3D84

Structural Analysis of a Holo Enzyme Complex of Mouse Dihydrofolate Reductase with NADPH and a Ternary Complex with the Potent and Selective Inhibitor 2.4-Diamino-6-(-2'-hydroxydibenz[b,f]azepin-5-yl)methylpteridine

Functional Information from GO Data

Chain	GOid	namespace	contents
X	0003723	molecular_function	RNA binding
X	0003729	molecular_function	mRNA binding
X	0004146	molecular_function	dihydrofolate reductase activity
X	0005634	cellular_component	nucleus
X	0005737	cellular_component	cytoplasm
X	0005739	cellular_component	mitochondrion
X	0005829	cellular_component	cytosol
X	0006231	biological_process	dTMP biosynthetic process
X	0006729	biological_process	tetrahydrobiopterin biosynthetic process
X	0006730	biological_process	one-carbon metabolic process
X	0008144	molecular_function	obsolete drug binding
X	0016491	molecular_function	oxidoreductase activity
X	0016646	molecular_function	oxidoreductase activity, acting on the CH-NH group of donors, NAD or NADP as acceptor
X	0031427	biological_process	response to methotrexate
X	0033560	molecular_function	folate reductase activity
X	0035999	biological_process	tetrahydrofolate interconversion
X	0046452	biological_process	dihydrofolate metabolic process
X	0046653	biological_process	tetrahydrofolate metabolic process
X	0046654	biological_process	tetrahydrofolate biosynthetic process
X	0046655	biological_process	folic acid metabolic process
X	0050661	molecular_function	NADP binding
X	2000121	biological_process	regulation of removal of superoxide radicals

Functional Information from PDB Data

site_id	AC1
Number of Residues	32
Details	BINDING SITE FOR RESIDUE NDP X 187

Chain	Residue
X	VAL8
X	GLY53
X	ARG54
X	LYS55
X	THR56
X	LEU75
X	SER76
X	ARG77
X	GLU78
X	LYS91
X	SER92
X	ALA9
X	VAL115
X	GLY117
X	SER118
X	SER119
X	VAL120
X	TYR121
X	GLU123
X	THR146
X	GOL188
X	HOH209
X	ILE16
X	HOH217
X	HOH221
X	HOH229
X	GLY17
X	LYS18
X	GLY20
X	ASP21
X	LEU22
X	TRP24

---

site_id	AC2
Number of Residues	8
Details	BINDING SITE FOR RESIDUE GOL X 188

Chain	Residue
X	ILE7
X	VAL8
X	ALA9
X	GLU30
X	PHE34
X	VAL115
X	TYR121
X	NDP187

---

site_id	AC3
Number of Residues	10
Details	BINDING SITE FOR RESIDUE GOL X 189

Chain	Residue
X	LEU158
X	LEU159
X	PRO160
X	GLU161
X	TYR162
X	VAL165
X	SER167
X	PHE179
X	GLU180
X	VAL181

---

Functional Information from PROSITE/UniProt

site_id	PS00075
Number of Residues	24
Details	DHFR_1 Dihydrofolate reductase (DHFR) domain signature. GIGkngdLPWpplrnEfkyFqrmT

Chain	Residue	Details
X	GLY15-THR38

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	181
Details	Domain: {"description":"DHFR","evidences":[{"source":"PROSITE-ProRule","id":"PRU00660","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	18
Details	Binding site: {"evidences":[{"source":"PubMed","id":"15681865","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17019704","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	7
Details	Binding site: {"evidences":[{"source":"PubMed","id":"15681865","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	1
Details	Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"PubMed","id":"23806337","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	Annotated By Reference To The Literature 1dhf

Chain	Residue	Details
X	LEU22
X	GLU30

---