Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3ZYV

Crystal structure of the mouse liver Aldehyde Oxidase 3 (mAOX3)

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004031	molecular_function	aldehyde oxidase activity
A	0005506	molecular_function	iron ion binding
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0006805	biological_process	xenobiotic metabolic process
A	0009055	molecular_function	electron transfer activity
A	0016491	molecular_function	oxidoreductase activity
A	0030151	molecular_function	molybdenum ion binding
A	0042803	molecular_function	protein homodimerization activity
A	0043546	molecular_function	molybdopterin cofactor binding
A	0046872	molecular_function	metal ion binding
A	0050660	molecular_function	flavin adenine dinucleotide binding
A	0051287	molecular_function	NAD binding
A	0051536	molecular_function	iron-sulfur cluster binding
A	0051537	molecular_function	2 iron, 2 sulfur cluster binding
A	0071949	molecular_function	FAD binding
B	0004031	molecular_function	aldehyde oxidase activity
B	0005506	molecular_function	iron ion binding
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0006805	biological_process	xenobiotic metabolic process
B	0009055	molecular_function	electron transfer activity
B	0016491	molecular_function	oxidoreductase activity
B	0030151	molecular_function	molybdenum ion binding
B	0042803	molecular_function	protein homodimerization activity
B	0043546	molecular_function	molybdopterin cofactor binding
B	0046872	molecular_function	metal ion binding
B	0050660	molecular_function	flavin adenine dinucleotide binding
B	0051287	molecular_function	NAD binding
B	0051536	molecular_function	iron-sulfur cluster binding
B	0051537	molecular_function	2 iron, 2 sulfur cluster binding
B	0071949	molecular_function	FAD binding
C	0004031	molecular_function	aldehyde oxidase activity
C	0005506	molecular_function	iron ion binding
C	0005737	cellular_component	cytoplasm
C	0005829	cellular_component	cytosol
C	0006805	biological_process	xenobiotic metabolic process
C	0009055	molecular_function	electron transfer activity
C	0016491	molecular_function	oxidoreductase activity
C	0030151	molecular_function	molybdenum ion binding
C	0042803	molecular_function	protein homodimerization activity
C	0043546	molecular_function	molybdopterin cofactor binding
C	0046872	molecular_function	metal ion binding
C	0050660	molecular_function	flavin adenine dinucleotide binding
C	0051287	molecular_function	NAD binding
C	0051536	molecular_function	iron-sulfur cluster binding
C	0051537	molecular_function	2 iron, 2 sulfur cluster binding
C	0071949	molecular_function	FAD binding
D	0004031	molecular_function	aldehyde oxidase activity
D	0005506	molecular_function	iron ion binding
D	0005737	cellular_component	cytoplasm
D	0005829	cellular_component	cytosol
D	0006805	biological_process	xenobiotic metabolic process
D	0009055	molecular_function	electron transfer activity
D	0016491	molecular_function	oxidoreductase activity
D	0030151	molecular_function	molybdenum ion binding
D	0042803	molecular_function	protein homodimerization activity
D	0043546	molecular_function	molybdopterin cofactor binding
D	0046872	molecular_function	metal ion binding
D	0050660	molecular_function	flavin adenine dinucleotide binding
D	0051287	molecular_function	NAD binding
D	0051536	molecular_function	iron-sulfur cluster binding
D	0051537	molecular_function	2 iron, 2 sulfur cluster binding
D	0071949	molecular_function	FAD binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE FES A 3001

Chain	Residue
A	CYS117
A	GLY118
A	CYS120
A	CYS152
A	CYS154

site_id	AC2
Number of Residues	8
Details	BINDING SITE FOR RESIDUE FES A 3002

Chain	Residue
A	CYS52
A	GLY53
A	CYS55
A	CYS77
A	CYS47
A	GLY48
A	GLY50
A	ASP51

site_id	AC3
Number of Residues	16
Details	BINDING SITE FOR RESIDUE MTE A 3003

Chain	Residue
A	GLN116
A	CYS154
A	ALA802
A	PHE803
A	ARG917
A	LEU1043
A	GLY1044
A	GLN1045
A	THR1082
A	GLY1083
A	ALA1084
A	SER1085
A	THR1086
A	GLY1087
A	GLN1199
A	MOS3004

site_id	AC4
Number of Residues	8
Details	BINDING SITE FOR RESIDUE MOS A 3004

Chain	Residue
A	GLN772
A	GLY804
A	PHE916
A	ARG917
A	ALA1084
A	GLU1266
A	HOH2181
A	MTE3003

site_id	AC5
Number of Residues	25
Details	BINDING SITE FOR RESIDUE FAD A 3005

Chain	Residue
A	GLY50
A	PRO263
A	LEU264
A	VAL265
A	ILE266
A	GLY267
A	ASN268
A	THR269
A	TYR270
A	LEU271
A	LEU294
A	THR308
A	LEU344
A	ALA345
A	ALA353
A	SER354
A	GLY357
A	HIS358
A	ILE360
A	SER366
A	ASP367
A	LEU411
A	ALA437
A	PHE438
A	HOH2182

site_id	AC6
Number of Residues	7
Details	BINDING SITE FOR RESIDUE FES B 3001

Chain	Residue
B	CYS117
B	GLY118
B	CYS120
B	CYS152
B	ARG153
B	CYS154
B	MET749

site_id	AC7
Number of Residues	8
Details	BINDING SITE FOR RESIDUE FES B 3002

Chain	Residue
B	CYS47
B	GLY48
B	GLY50
B	ASP51
B	CYS52
B	GLY53
B	CYS55
B	CYS77

site_id	AC8
Number of Residues	17
Details	BINDING SITE FOR RESIDUE MTE B 3003

Chain	Residue
B	GLN116
B	CYS154
B	ALA802
B	PHE803
B	ARG917
B	LEU1043
B	GLY1044
B	GLN1045
B	THR1082
B	GLY1083
B	ALA1084
B	SER1085
B	THR1086
B	GLY1087
B	GLN1199
B	HOH2145
B	MOS3004

site_id	AC9
Number of Residues	7
Details	BINDING SITE FOR RESIDUE MOS B 3004

Chain	Residue
B	GLU1266
B	MTE3003
B	GLN772
B	GLY804
B	PHE916
B	ARG917
B	ALA1084

site_id	BC1
Number of Residues	23
Details	BINDING SITE FOR RESIDUE FAD B 3005

Chain	Residue
B	GLY50
B	LEU264
B	VAL265
B	ILE266
B	GLY267
B	ASN268
B	THR269
B	TYR270
B	LEU271
B	LEU294
B	THR308
B	LEU344
B	ALA353
B	SER354
B	GLY357
B	HIS358
B	ILE360
B	SER366
B	ASP367
B	LEU411
B	ALA437
B	PHE438
B	HOH2166

site_id	BC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE FES C 3001

Chain	Residue
C	GLN116
C	CYS117
C	GLY118
C	CYS120
C	CYS152
C	ARG153
C	CYS154

site_id	BC3
Number of Residues	8
Details	BINDING SITE FOR RESIDUE FES C 3002

Chain	Residue
C	CYS47
C	GLY48
C	GLY50
C	ASP51
C	CYS52
C	GLY53
C	CYS55
C	CYS77

site_id	BC4
Number of Residues	20
Details	BINDING SITE FOR RESIDUE MTE C 3003

Chain	Residue
C	GLN116
C	CYS154
C	GLY801
C	ALA802
C	PHE803
C	GLY804
C	ARG917
C	LEU1043
C	GLY1044
C	GLN1045
C	THR1082
C	GLY1083
C	ALA1084
C	SER1085
C	THR1086
C	GLY1087
C	GLN1199
C	HOH2021
C	HOH2130
C	MOS3004

site_id	BC5
Number of Residues	7
Details	BINDING SITE FOR RESIDUE MOS C 3004

Chain	Residue
C	GLN772
C	GLY804
C	PHE916
C	ARG917
C	ALA1084
C	GLU1266
C	MTE3003

site_id	BC6
Number of Residues	23
Details	BINDING SITE FOR RESIDUE FAD C 3005

Chain	Residue
C	LEU264
C	VAL265
C	ILE266
C	GLY267
C	ASN268
C	THR269
C	TYR270
C	LEU271
C	THR308
C	LEU312
C	LEU344
C	SER354
C	GLY357
C	HIS358
C	ILE360
C	SER366
C	ASP367
C	LEU411
C	ARG429
C	ALA437
C	PHE438
C	HOH2057
C	HOH2146

site_id	BC7
Number of Residues	6
Details	BINDING SITE FOR RESIDUE FES D 3001

Chain	Residue
D	CYS117
D	GLY118
D	CYS120
D	CYS152
D	ARG153
D	CYS154

site_id	BC8
Number of Residues	8
Details	BINDING SITE FOR RESIDUE FES D 3002

Chain	Residue
D	CYS47
D	GLY48
D	GLY50
D	ASP51
D	CYS52
D	GLY53
D	CYS55
D	CYS77

site_id	BC9
Number of Residues	14
Details	BINDING SITE FOR RESIDUE MTE D 3003

Chain	Residue
D	GLN116
D	CYS154
D	GLY801
D	ALA802
D	PHE803
D	ARG917
D	LEU1043
D	GLY1044
D	GLN1045
D	GLY1083
D	SER1085
D	GLY1087
D	GLN1199
D	MOS3004

site_id	CC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE MOS D 3004

Chain	Residue
D	GLN772
D	GLY804
D	PHE916
D	ARG917
D	ALA1084
D	GLU1266
D	MTE3003

site_id	CC2
Number of Residues	25
Details	BINDING SITE FOR RESIDUE FAD D 3005

Chain	Residue
D	GLY49
D	GLY50
D	PRO263
D	LEU264
D	ILE266
D	GLY267
D	ASN268
D	THR269
D	TYR270
D	LEU271
D	LEU294
D	THR308
D	LEU344
D	ALA353
D	SER354
D	GLY357
D	HIS358
D	ILE360
D	SER366
D	ASP367
D	VAL410
D	LEU411
D	ALA437
D	PHE438
D	HOH2061

site_id	CC3
Number of Residues	7
Details	BINDING SITE FOR RESIDUE NA A 2337

Chain	Residue
A	GLY872
A	THR875
A	PRO876
A	ASP877
A	SER879
A	SER912
A	ASN913

site_id	CC4
Number of Residues	8
Details	BINDING SITE FOR RESIDUE NA B 2337

Chain	Residue
B	GLY872
B	THR875
B	PRO876
B	ASP877
B	SER879
B	SER912
B	ASN913
B	HOH2124

site_id	CC5
Number of Residues	7
Details	BINDING SITE FOR RESIDUE NA D 2337

Chain	Residue
D	GLY872
D	THR875
D	PRO876
D	ASP877
D	SER879
D	SER912
D	ASN913

site_id	CC6
Number of Residues	7
Details	BINDING SITE FOR RESIDUE NA C 2337

Chain	Residue
C	GLY872
C	THR875
C	PRO876
C	ASP877
C	SER879
C	SER912
C	ASN913

Functional Information from PROSITE/UniProt

site_id	PS00197
Number of Residues	9
Details	2FE2S_FER_1 2Fe-2S ferredoxin-type iron-sulfur binding region signature. CGGGDCGAC

Chain	Residue	Details
A	CYS47-CYS55

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	348
Details	Domain: {"description":"2Fe-2S ferredoxin-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00465","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	4
Details	Active site: {"description":"Proton acceptor; for azaheterocycle hydroxylase activity","evidences":[{"source":"PubMed","id":"23019336","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	92
Details	Binding site: {"evidences":[{"source":"PubMed","id":"23019336","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	4
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q5QE80","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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