Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6AD4

Rat Xanthine oxidoreductase, D428A variant, NADH bound form

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000255	biological_process	allantoin metabolic process
A	0004854	molecular_function	xanthine dehydrogenase activity
A	0004855	molecular_function	xanthine oxidase activity
A	0005506	molecular_function	iron ion binding
A	0005576	cellular_component	extracellular region
A	0005615	cellular_component	extracellular space
A	0005737	cellular_component	cytoplasm
A	0005777	cellular_component	peroxisome
A	0005829	cellular_component	cytosol
A	0006147	biological_process	guanine catabolic process
A	0006148	biological_process	inosine catabolic process
A	0006149	biological_process	deoxyinosine catabolic process
A	0006154	biological_process	adenosine catabolic process
A	0006157	biological_process	deoxyadenosine catabolic process
A	0006161	biological_process	deoxyguanosine catabolic process
A	0006196	biological_process	AMP catabolic process
A	0006204	biological_process	IMP catabolic process
A	0007595	biological_process	lactation
A	0009114	biological_process	hypoxanthine catabolic process
A	0009115	biological_process	xanthine catabolic process
A	0010044	biological_process	response to aluminum ion
A	0016226	biological_process	iron-sulfur cluster assembly
A	0016491	molecular_function	oxidoreductase activity
A	0016529	cellular_component	sarcoplasmic reticulum
A	0030856	biological_process	regulation of epithelial cell differentiation
A	0032496	biological_process	response to lipopolysaccharide
A	0034465	biological_process	response to carbon monoxide
A	0042542	biological_process	response to hydrogen peroxide
A	0042802	molecular_function	identical protein binding
A	0042803	molecular_function	protein homodimerization activity
A	0043546	molecular_function	molybdopterin cofactor binding
A	0043605	biological_process	amide catabolic process
A	0046038	biological_process	GMP catabolic process
A	0046055	biological_process	dGMP catabolic process
A	0046059	biological_process	dAMP catabolic process
A	0046872	molecular_function	metal ion binding
A	0050421	molecular_function	nitrite reductase (NO-forming) activity
A	0050660	molecular_function	flavin adenine dinucleotide binding
A	0051536	molecular_function	iron-sulfur cluster binding
A	0051537	molecular_function	2 iron, 2 sulfur cluster binding
A	0070674	molecular_function	hypoxanthine dehydrogenase activity
A	0070675	molecular_function	hypoxanthine oxidase activity
A	0071347	biological_process	cellular response to interleukin-1
A	0071356	biological_process	cellular response to tumor necrosis factor
A	0071949	molecular_function	FAD binding
A	0097184	biological_process	response to azide
B	0000255	biological_process	allantoin metabolic process
B	0004854	molecular_function	xanthine dehydrogenase activity
B	0004855	molecular_function	xanthine oxidase activity
B	0005506	molecular_function	iron ion binding
B	0005576	cellular_component	extracellular region
B	0005615	cellular_component	extracellular space
B	0005737	cellular_component	cytoplasm
B	0005777	cellular_component	peroxisome
B	0005829	cellular_component	cytosol
B	0006147	biological_process	guanine catabolic process
B	0006148	biological_process	inosine catabolic process
B	0006149	biological_process	deoxyinosine catabolic process
B	0006154	biological_process	adenosine catabolic process
B	0006157	biological_process	deoxyadenosine catabolic process
B	0006161	biological_process	deoxyguanosine catabolic process
B	0006196	biological_process	AMP catabolic process
B	0006204	biological_process	IMP catabolic process
B	0007595	biological_process	lactation
B	0009114	biological_process	hypoxanthine catabolic process
B	0009115	biological_process	xanthine catabolic process
B	0010044	biological_process	response to aluminum ion
B	0016226	biological_process	iron-sulfur cluster assembly
B	0016491	molecular_function	oxidoreductase activity
B	0016529	cellular_component	sarcoplasmic reticulum
B	0030856	biological_process	regulation of epithelial cell differentiation
B	0032496	biological_process	response to lipopolysaccharide
B	0034465	biological_process	response to carbon monoxide
B	0042542	biological_process	response to hydrogen peroxide
B	0042802	molecular_function	identical protein binding
B	0042803	molecular_function	protein homodimerization activity
B	0043546	molecular_function	molybdopterin cofactor binding
B	0043605	biological_process	amide catabolic process
B	0046038	biological_process	GMP catabolic process
B	0046055	biological_process	dGMP catabolic process
B	0046059	biological_process	dAMP catabolic process
B	0046872	molecular_function	metal ion binding
B	0050421	molecular_function	nitrite reductase (NO-forming) activity
B	0050660	molecular_function	flavin adenine dinucleotide binding
B	0051536	molecular_function	iron-sulfur cluster binding
B	0051537	molecular_function	2 iron, 2 sulfur cluster binding
B	0070674	molecular_function	hypoxanthine dehydrogenase activity
B	0070675	molecular_function	hypoxanthine oxidase activity
B	0071347	biological_process	cellular response to interleukin-1
B	0071356	biological_process	cellular response to tumor necrosis factor
B	0071949	molecular_function	FAD binding
B	0097184	biological_process	response to azide

Functional Information from PDB Data

site_id	AC1
Number of Residues	10
Details	binding site for residue URC A 1501

Chain	Residue
A	GLU802
A	HOH2011
A	ARG880
A	PHE914
A	PHE1009
A	THR1010
A	ALA1078
A	ALA1079
A	GLU1261
A	HOH1726

site_id	AC2
Number of Residues	9
Details	binding site for residue BCT A 1502

Chain	Residue
A	ARG839
A	HIS840
A	ILE877
A	THR909
A	ALA910
A	PHE911
A	PHE914
A	GLY915
A	GLN918

site_id	AC3
Number of Residues	10
Details	binding site for residue FES A 1503

Chain	Residue
A	GLY42
A	CYS43
A	GLY44
A	GLY46
A	GLY47
A	CYS48
A	GLY49
A	CYS51
A	ASN71
A	CYS73

site_id	AC4
Number of Residues	8
Details	binding site for residue FES A 1504

Chain	Residue
A	GLN111
A	CYS112
A	GLY113
A	CYS115
A	CYS147
A	ARG148
A	CYS149
A	LEU744

site_id	AC5
Number of Residues	30
Details	binding site for residue FAD A 1505

Chain	Residue
A	GLU45
A	GLY46
A	LYS255
A	LEU256
A	VAL257
A	VAL258
A	GLY259
A	ASN260
A	THR261
A	GLU262
A	ILE263
A	ALA300
A	PHE336
A	ALA337
A	ALA345
A	SER346
A	GLY349
A	ASN350
A	ILE352
A	THR353
A	SER358
A	ASP359
A	LEU403
A	LYS421
A	NAI1506
A	HOH1601
A	HOH1672
A	HOH1887
A	HOH1902
A	HOH1918

site_id	AC6
Number of Residues	20
Details	binding site for residue NAI A 1506

Chain	Residue
A	GLU262
A	SER355
A	PRO356
A	ILE357
A	TYR392
A	ARG393
A	ALA428
A	ASP429
A	ILE430
A	GLY457
A	ALA459
A	PRO500
A	ARG507
A	SER1225
A	FAD1505
A	HOH1601
A	HOH1685
A	HOH1717
A	HOH1732
A	HOH1887

site_id	AC7
Number of Residues	8
Details	binding site for residue FES B 3001

Chain	Residue
B	GLN111
B	CYS112
B	GLY113
B	CYS115
B	CYS147
B	ARG148
B	CYS149
B	LEU744

site_id	AC8
Number of Residues	10
Details	binding site for residue FES B 3002

Chain	Residue
B	GLY47
B	CYS48
B	GLY49
B	CYS51
B	ASN71
B	CYS73
B	GLY42
B	CYS43
B	GLY44
B	GLY46

site_id	AC9
Number of Residues	10
Details	binding site for residue URC B 3003

Chain	Residue
B	GLU802
B	ARG880
B	PHE914
B	PHE1009
B	THR1010
B	ALA1078
B	ALA1079
B	GLU1261
B	HOH3404
B	HOH3485

site_id	AD1
Number of Residues	9
Details	binding site for residue BCT B 3004

Chain	Residue
B	ARG839
B	HIS840
B	ILE877
B	THR909
B	ALA910
B	PHE911
B	PHE914
B	GLY915
B	GLN918

site_id	AD2
Number of Residues	31
Details	binding site for residue FAD B 3005

Chain	Residue
B	GLU45
B	GLY46
B	LYS255
B	LEU256
B	VAL257
B	VAL258
B	GLY259
B	ASN260
B	THR261
B	GLU262
B	ILE263
B	ALA300
B	PHE336
B	ALA337
B	VAL341
B	ALA345
B	SER346
B	GLY349
B	ASN350
B	ILE352
B	THR353
B	SER358
B	ASP359
B	LEU403
B	LYS421
B	NAI3006
B	HOH3227
B	HOH3325
B	HOH3391
B	HOH3440
B	HOH3585

site_id	AD3
Number of Residues	22
Details	binding site for residue NAI B 3006

Chain	Residue
B	GLU262
B	LYS270
B	SER355
B	PRO356
B	ILE357
B	TYR392
B	ARG393
B	ASP429
B	ILE430
B	GLY457
B	ALA459
B	ASP460
B	PRO500
B	GLY501
B	ARG507
B	SER1225
B	FAD3005
B	HOH3135
B	HOH3377
B	HOH3391
B	HOH3471
B	HOH3677

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. CGEGGCGAC

Chain	Residue	Details
A	CYS43-CYS51

site_id	PS00559
Number of Residues	36
Details	MOLYBDOPTERIN_EUK Eukaryotic molybdopterin oxidoreductases signature. GFggKetrstvvstala..LaahKTgrpVrCmlDRdeD

Chain	Residue	Details
A	GLY797-ASP832

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	174
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	370
Details	Domain: {"description":"FAD-binding PCMH-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00718","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	2
Details	Active site: {"description":"Proton acceptor"}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	16
Details	Binding site: {"evidences":[{"source":"PubMed","id":"17301076","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2E3T","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	26
Details	Binding site: {"evidences":[{"source":"PubMed","id":"15878860","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17301076","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details