3NXT

Preferential Selection of Isomer Binding from Chiral Mixtures: Alternate Binding Modes Observed for the E-and Z-isomers of a Series of 5-substituted 2,4-diaminofuro[2m,3-d]pyrimidines as Ternary Complexes with NADPH and Human Dihydrofolate Reductase

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000900	molecular_function	mRNA regulatory element binding translation repressor activity
A	0003723	molecular_function	RNA binding
A	0003729	molecular_function	mRNA binding
A	0004146	molecular_function	dihydrofolate reductase activity
A	0005515	molecular_function	protein binding
A	0005542	molecular_function	folic acid binding
A	0005737	cellular_component	cytoplasm
A	0005739	cellular_component	mitochondrion
A	0005829	cellular_component	cytosol
A	0006729	biological_process	tetrahydrobiopterin biosynthetic process
A	0006730	biological_process	one-carbon metabolic process
A	0008144	molecular_function	obsolete drug binding
A	0016491	molecular_function	oxidoreductase activity
A	0017148	biological_process	negative regulation of translation
A	0031103	biological_process	axon regeneration
A	0031427	biological_process	response to methotrexate
A	0046452	biological_process	dihydrofolate metabolic process
A	0046653	biological_process	tetrahydrofolate metabolic process
A	0046654	biological_process	tetrahydrofolate biosynthetic process
A	0046655	biological_process	folic acid metabolic process
A	0050661	molecular_function	NADP binding
A	0060090	molecular_function	molecular adaptor activity
A	0070402	molecular_function	NADPH binding
A	1990825	molecular_function	sequence-specific mRNA binding
A	2000121	biological_process	regulation of removal of superoxide radicals

Functional Information from PDB Data

site_id	AC1
Number of Residues	35
Details	BINDING SITE FOR RESIDUE NDP A 187

Chain	Residue
A	VAL8
A	LYS54
A	LYS55
A	THR56
A	LEU75
A	SER76
A	ARG77
A	GLU78
A	ARG91
A	SER92
A	VAL115
A	ALA9
A	GLY116
A	GLY117
A	SER118
A	SER119
A	VAL120
A	TYR121
A	GLU123
A	THR146
A	D2E188
A	SO4191
A	ILE16
A	HOH210
A	HOH227
A	HOH241
A	HOH283
A	HOH305
A	HOH310
A	GLY17
A	LYS18
A	GLY20
A	ASP21
A	LEU22
A	GLY53

---

site_id	AC2
Number of Residues	15
Details	BINDING SITE FOR RESIDUE D2E A 188

Chain	Residue
A	ILE7
A	VAL8
A	ALA9
A	LEU22
A	GLU30
A	PHE31
A	PHE34
A	THR56
A	SER59
A	ILE60
A	LEU67
A	VAL115
A	THR136
A	NDP187
A	HOH255

---

site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 A 189

Chain	Residue
A	GLU143
A	VAL165
A	LEU166
A	SER167
A	HOH284

---

site_id	AC4
Number of Residues	2
Details	BINDING SITE FOR RESIDUE SO4 A 190

Chain	Residue
A	GLU62
A	ARG65

---

site_id	AC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 A 191

Chain	Residue
A	SER118
A	THR146
A	LYS178
A	NDP187
A	HOH213
A	HOH278

---

site_id	AC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 A 192

Chain	Residue
A	LYS122
A	PRO149
A	GLU150
A	HOH300

---

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	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":"15039552","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16222560","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19478082","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	7
Details	Binding site: {"evidences":[{"source":"PubMed","id":"2248959","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	2
Details	M-CSA 490

Chain	Residue	Details
A	LEU22	electrostatic stabiliser
A	GLU30	electrostatic stabiliser

---