Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3TZB

Quinone Oxidoreductase (NQ02) bound to NSC13000

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 231

Chain	Residue
A	HIS173
A	HIS177
A	CYS222

site_id	AC2
Number of Residues	24
Details	BINDING SITE FOR RESIDUE FAD A 232

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	HOH266
A	HOH373
B	ASN66
B	ASP117
B	AA501
A	HIS11
A	LYS15
A	SER16
A	PHE17
A	ASN18
A	SER20

site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE AA A 501

Chain	Residue
A	PHE126
A	PHE178
B	TRP105
B	FAD232

site_id	AC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE ZN B 231

Chain	Residue
B	HIS173
B	HIS177
B	CYS222

site_id	AC5
Number of Residues	23
Details	BINDING SITE FOR RESIDUE FAD B 232

Chain	Residue
A	ASN66
A	ASP117
A	AA501
B	HIS11
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	VAL204
B	HOH250
B	HOH286

site_id	AC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE AA B 501

Chain	Residue
A	TRP105
A	FAD232
B	PHE126
B	PHE178

site_id	AC7
Number of Residues	3
Details	BINDING SITE FOR RESIDUE ZN C 231

Chain	Residue
C	HIS173
C	HIS177
C	CYS222

site_id	AC8
Number of Residues	23
Details	BINDING SITE FOR RESIDUE FAD C 232

Chain	Residue
C	HIS11
C	LYS15
C	SER16
C	PHE17
C	ASN18
C	SER20
C	PRO102
C	LEU103
C	TYR104
C	TRP105
C	PHE106
C	THR147
C	THR148
C	GLY149
C	GLY150
C	TYR155
C	GLU193
C	ARG200
C	HOH305
C	HOH318
C	AA501
D	ASP117
D	HOH275

site_id	AC9
Number of Residues	6
Details	BINDING SITE FOR RESIDUE AA C 501

Chain	Residue
A	MET1
C	TRP105
C	FAD232
D	LEU120
D	PHE126
D	PHE178

site_id	BC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE ZN D 231

Chain	Residue
D	HIS173
D	HIS177
D	CYS222

site_id	BC2
Number of Residues	26
Details	BINDING SITE FOR RESIDUE FAD D 232

Chain	Residue
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	GLU197
D	ARG200
D	HOH280
D	HOH289
D	HOH299
D	HOH310
C	ASN66
C	ASP117
C	AA230

site_id	BC3
Number of Residues	7
Details	BINDING SITE FOR RESIDUE AA C 230

Chain	Residue
C	GLN122
C	PHE126
C	PHE178
C	HOH293
D	TRP105
D	PHE106
D	FAD232

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)