Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4FGL

Reduced quinone reductase 2 in complex with chloroquine

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0001512	molecular_function	dihydronicotinamide riboside quinone reductase activity
A	0003955	molecular_function	NAD(P)H dehydrogenase (quinone) activity
A	0005515	molecular_function	protein binding
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0008270	molecular_function	zinc ion binding
A	0009055	molecular_function	electron transfer activity
A	0016491	molecular_function	oxidoreductase activity
A	0016661	molecular_function	oxidoreductase activity, acting on other nitrogenous compounds as donors
A	0031404	molecular_function	chloride ion binding
A	0042803	molecular_function	protein homodimerization activity
A	0046872	molecular_function	metal ion binding
A	0070062	cellular_component	extracellular exosome
A	0071949	molecular_function	FAD binding
A	1901662	biological_process	quinone catabolic process
A	1904408	molecular_function	melatonin binding
A	1905594	molecular_function	resveratrol binding
B	0001512	molecular_function	dihydronicotinamide riboside quinone reductase activity
B	0003955	molecular_function	NAD(P)H dehydrogenase (quinone) activity
B	0005515	molecular_function	protein binding
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0008270	molecular_function	zinc ion binding
B	0009055	molecular_function	electron transfer activity
B	0016491	molecular_function	oxidoreductase activity
B	0016661	molecular_function	oxidoreductase activity, acting on other nitrogenous compounds as donors
B	0031404	molecular_function	chloride ion binding
B	0042803	molecular_function	protein homodimerization activity
B	0046872	molecular_function	metal ion binding
B	0070062	cellular_component	extracellular exosome
B	0071949	molecular_function	FAD binding
B	1901662	biological_process	quinone catabolic process
B	1904408	molecular_function	melatonin binding
B	1905594	molecular_function	resveratrol binding
C	0001512	molecular_function	dihydronicotinamide riboside quinone reductase activity
C	0003955	molecular_function	NAD(P)H dehydrogenase (quinone) activity
C	0005515	molecular_function	protein binding
C	0005737	cellular_component	cytoplasm
C	0005829	cellular_component	cytosol
C	0008270	molecular_function	zinc ion binding
C	0009055	molecular_function	electron transfer activity
C	0016491	molecular_function	oxidoreductase activity
C	0016661	molecular_function	oxidoreductase activity, acting on other nitrogenous compounds as donors
C	0031404	molecular_function	chloride ion binding
C	0042803	molecular_function	protein homodimerization activity
C	0046872	molecular_function	metal ion binding
C	0070062	cellular_component	extracellular exosome
C	0071949	molecular_function	FAD binding
C	1901662	biological_process	quinone catabolic process
C	1904408	molecular_function	melatonin binding
C	1905594	molecular_function	resveratrol binding
D	0001512	molecular_function	dihydronicotinamide riboside quinone reductase activity
D	0003955	molecular_function	NAD(P)H dehydrogenase (quinone) activity
D	0005515	molecular_function	protein binding
D	0005737	cellular_component	cytoplasm
D	0005829	cellular_component	cytosol
D	0008270	molecular_function	zinc ion binding
D	0009055	molecular_function	electron transfer activity
D	0016491	molecular_function	oxidoreductase activity
D	0016661	molecular_function	oxidoreductase activity, acting on other nitrogenous compounds as donors
D	0031404	molecular_function	chloride ion binding
D	0042803	molecular_function	protein homodimerization activity
D	0046872	molecular_function	metal ion binding
D	0070062	cellular_component	extracellular exosome
D	0071949	molecular_function	FAD binding
D	1901662	biological_process	quinone catabolic process
D	1904408	molecular_function	melatonin binding
D	1905594	molecular_function	resveratrol binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE ZN A 301

Chain	Residue
A	HIS173
A	HIS177
A	CYS222

site_id	AC2
Number of Residues	33
Details	BINDING SITE FOR RESIDUE FAD A 302

Chain	Residue
A	PRO102
A	LEU103
A	TYR104
A	TRP105
A	PHE106
A	THR147
A	THR148
A	GLY149
A	GLY150
A	TYR155
A	GLU193
A	GLU197
A	ARG200
A	LYS201
A	CLQ303
A	HOH415
A	HOH430
A	HOH439
A	HOH452
A	HOH453
A	HOH505
A	HOH571
A	HOH657
A	HOH684
B	ASN66
B	ASP117
B	HOH427
A	HIS11
A	LYS15
A	SER16
A	PHE17
A	ASN18
A	SER20

site_id	AC3
Number of Residues	10
Details	BINDING SITE FOR RESIDUE CLQ A 303

Chain	Residue
A	GLY149
A	GLY150
A	ASN161
A	GLU193
A	FAD302
A	HOH415
B	PHE126
B	ILE128
B	PHE178
B	HOH595

site_id	AC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE ZN B 301

Chain	Residue
B	HIS173
B	HIS177
B	CYS222

site_id	AC5
Number of Residues	31
Details	BINDING SITE FOR RESIDUE FAD B 302

Chain	Residue
A	ASP117
A	HOH547
B	HIS11
B	LYS15
B	SER16
B	PHE17
B	ASN18
B	SER20
B	PRO102
B	LEU103
B	TYR104
B	TRP105
B	PHE106
B	THR147
B	THR148
B	GLY149
B	GLY150
B	TYR155
B	GLU193
B	ARG200
B	LYS201
B	CLQ303
B	HOH428
B	HOH439
B	HOH461
B	HOH464
B	HOH475
B	HOH486
B	HOH497
B	HOH561
B	HOH672

site_id	AC6
Number of Residues	8
Details	BINDING SITE FOR RESIDUE CLQ B 303

Chain	Residue
A	GLN122
A	PHE126
A	PHE178
B	GLY150
B	ASN161
B	GLU193
B	FAD302
B	HOH478

site_id	AC7
Number of Residues	3
Details	BINDING SITE FOR RESIDUE ZN C 301

Chain	Residue
C	HIS173
C	HIS177
C	CYS222

site_id	AC8
Number of Residues	28
Details	BINDING SITE FOR RESIDUE FAD C 302

Chain	Residue
C	TYR104
C	TRP105
C	PHE106
C	THR147
C	THR148
C	GLY149
C	GLY150
C	TYR155
C	GLU193
C	ARG200
C	LYS201
C	CLQ303
C	HOH439
C	HOH451
C	HOH458
C	HOH488
C	HOH490
C	HOH573
C	HOH605
D	ASP117
C	HIS11
C	LYS15
C	SER16
C	PHE17
C	ASN18
C	SER20
C	PRO102
C	LEU103

site_id	AC9
Number of Residues	12
Details	BINDING SITE FOR RESIDUE CLQ C 303

Chain	Residue
C	GLU73
C	GLY149
C	GLY150
C	MET154
C	FAD302
C	HOH451
C	HOH484
C	HOH557
D	GLN122
D	PHE126
D	ILE128
D	PHE178

site_id	BC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE ZN D 301

Chain	Residue
D	HIS173
D	HIS177
D	CYS222

site_id	BC2
Number of Residues	28
Details	BINDING SITE FOR RESIDUE FAD D 302

Chain	Residue
C	ASP117
D	HIS11
D	LYS15
D	SER16
D	PHE17
D	ASN18
D	SER20
D	PRO102
D	LEU103
D	TYR104
D	TRP105
D	PHE106
D	THR147
D	THR148
D	GLY149
D	GLY150
D	TYR155
D	GLU193
D	ARG200
D	LYS201
D	CLQ303
D	HOH407
D	HOH429
D	HOH472
D	HOH489
D	HOH507
D	HOH510
D	HOH566

site_id	BC3
Number of Residues	12
Details	BINDING SITE FOR RESIDUE CLQ D 303

Chain	Residue
C	GLN122
C	PHE126
C	ILE128
C	PHE178
C	HOH639
D	GLY149
D	GLY150
D	MET154
D	GLU193
D	FAD302
D	HOH413
D	HOH479

site_id	BC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CLQ D 304

Chain	Residue
D	LYS22
D	ASN23
D	VAL26
D	ASP27

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	52
Details	Binding site: {"evidences":[{"source":"PubMed","id":"18254726","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19236722","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	20
Details	Binding site: {}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	8
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"19369195","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)