Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2CKJ

Human milk xanthine oxidoreductase

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	0005515	molecular_function	protein 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	0009114	biological_process	hypoxanthine catabolic process
A	0009115	biological_process	xanthine catabolic process
A	0016491	molecular_function	oxidoreductase activity
A	0016529	cellular_component	sarcoplasmic reticulum
A	0042803	molecular_function	protein homodimerization activity
A	0043546	molecular_function	molybdopterin cofactor binding
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	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	0071949	molecular_function	FAD binding
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	0005515	molecular_function	protein 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	0009114	biological_process	hypoxanthine catabolic process
B	0009115	biological_process	xanthine catabolic process
B	0016491	molecular_function	oxidoreductase activity
B	0016529	cellular_component	sarcoplasmic reticulum
B	0042803	molecular_function	protein homodimerization activity
B	0043546	molecular_function	molybdopterin cofactor binding
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	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	0071949	molecular_function	FAD binding
C	0000255	biological_process	allantoin metabolic process
C	0004854	molecular_function	xanthine dehydrogenase activity
C	0004855	molecular_function	xanthine oxidase activity
C	0005506	molecular_function	iron ion binding
C	0005515	molecular_function	protein binding
C	0005576	cellular_component	extracellular region
C	0005615	cellular_component	extracellular space
C	0005737	cellular_component	cytoplasm
C	0005777	cellular_component	peroxisome
C	0005829	cellular_component	cytosol
C	0006147	biological_process	guanine catabolic process
C	0006148	biological_process	inosine catabolic process
C	0006149	biological_process	deoxyinosine catabolic process
C	0006154	biological_process	adenosine catabolic process
C	0006157	biological_process	deoxyadenosine catabolic process
C	0006161	biological_process	deoxyguanosine catabolic process
C	0006196	biological_process	AMP catabolic process
C	0006204	biological_process	IMP catabolic process
C	0009114	biological_process	hypoxanthine catabolic process
C	0009115	biological_process	xanthine catabolic process
C	0016491	molecular_function	oxidoreductase activity
C	0016529	cellular_component	sarcoplasmic reticulum
C	0042803	molecular_function	protein homodimerization activity
C	0043546	molecular_function	molybdopterin cofactor binding
C	0046038	biological_process	GMP catabolic process
C	0046055	biological_process	dGMP catabolic process
C	0046059	biological_process	dAMP catabolic process
C	0046872	molecular_function	metal ion binding
C	0050660	molecular_function	flavin adenine dinucleotide binding
C	0051536	molecular_function	iron-sulfur cluster binding
C	0051537	molecular_function	2 iron, 2 sulfur cluster binding
C	0070674	molecular_function	hypoxanthine dehydrogenase activity
C	0070675	molecular_function	hypoxanthine oxidase activity
C	0071949	molecular_function	FAD binding
D	0000255	biological_process	allantoin metabolic process
D	0004854	molecular_function	xanthine dehydrogenase activity
D	0004855	molecular_function	xanthine oxidase activity
D	0005506	molecular_function	iron ion binding
D	0005515	molecular_function	protein binding
D	0005576	cellular_component	extracellular region
D	0005615	cellular_component	extracellular space
D	0005737	cellular_component	cytoplasm
D	0005777	cellular_component	peroxisome
D	0005829	cellular_component	cytosol
D	0006147	biological_process	guanine catabolic process
D	0006148	biological_process	inosine catabolic process
D	0006149	biological_process	deoxyinosine catabolic process
D	0006154	biological_process	adenosine catabolic process
D	0006157	biological_process	deoxyadenosine catabolic process
D	0006161	biological_process	deoxyguanosine catabolic process
D	0006196	biological_process	AMP catabolic process
D	0006204	biological_process	IMP catabolic process
D	0009114	biological_process	hypoxanthine catabolic process
D	0009115	biological_process	xanthine catabolic process
D	0016491	molecular_function	oxidoreductase activity
D	0016529	cellular_component	sarcoplasmic reticulum
D	0042803	molecular_function	protein homodimerization activity
D	0043546	molecular_function	molybdopterin cofactor binding
D	0046038	biological_process	GMP catabolic process
D	0046055	biological_process	dGMP catabolic process
D	0046059	biological_process	dAMP catabolic process
D	0046872	molecular_function	metal ion binding
D	0050660	molecular_function	flavin adenine dinucleotide binding
D	0051536	molecular_function	iron-sulfur cluster binding
D	0051537	molecular_function	2 iron, 2 sulfur cluster binding
D	0070674	molecular_function	hypoxanthine dehydrogenase activity
D	0070675	molecular_function	hypoxanthine oxidase activity
D	0071949	molecular_function	FAD binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE PO4 D3009

Chain	Residue
D	GLN1041
D	ALA1079
D	SER1081
D	SER1083
D	GLY1261
D	ACY3008

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE FES A3001

Chain	Residue
A	CYS148
A	ARG149
A	CYS150
A	CYS113
A	GLY114
A	CYS116

site_id	AC3
Number of Residues	8
Details	BINDING SITE FOR RESIDUE FES A3002

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

site_id	AC4
Number of Residues	23
Details	BINDING SITE FOR RESIDUE FAD A3006

Chain	Residue
A	GLY46
A	LYS256
A	LEU257
A	VAL258
A	VAL259
A	GLY260
A	ASN261
A	THR262
A	GLU263
A	ILE264
A	PHE337
A	ALA338
A	ALA346
A	SER347
A	GLY350
A	ASN351
A	ILE353
A	THR354
A	SER359
A	ASP360
A	ILE403
A	LEU404
A	LYS422

site_id	AC5
Number of Residues	7
Details	BINDING SITE FOR RESIDUE FES B3001

Chain	Residue
B	GLN112
B	CYS113
B	GLY114
B	CYS116
B	CYS148
B	ARG149
B	CYS150

site_id	AC6
Number of Residues	8
Details	BINDING SITE FOR RESIDUE FES B3002

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

site_id	AC7
Number of Residues	20
Details	BINDING SITE FOR RESIDUE FAD B3006

Chain	Residue
B	LYS256
B	LEU257
B	VAL259
B	GLY260
B	ASN261
B	THR262
B	GLU263
B	ILE264
B	PHE337
B	ALA338
B	ALA346
B	SER347
B	GLY350
B	ASN351
B	ILE353
B	THR354
B	SER359
B	ASP360
B	LEU404
B	LYS422

site_id	AC8
Number of Residues	7
Details	BINDING SITE FOR RESIDUE FES C3001

Chain	Residue
C	GLN112
C	CYS113
C	GLY114
C	CYS116
C	CYS148
C	ARG149
C	CYS150

site_id	AC9
Number of Residues	8
Details	BINDING SITE FOR RESIDUE FES C3002

Chain	Residue
C	GLY42
C	CYS43
C	GLY44
C	GLY46
C	CYS48
C	GLY49
C	CYS51
C	CYS73

site_id	BC1
Number of Residues	22
Details	BINDING SITE FOR RESIDUE FAD C3006

Chain	Residue
C	THR262
C	GLU263
C	ILE264
C	ALA301
C	PHE337
C	ALA338
C	ALA346
C	SER347
C	GLY350
C	ASN351
C	ILE353
C	SER359
C	ASP360
C	ILE403
C	LEU404
C	LYS422
C	GLY46
C	LYS256
C	LEU257
C	VAL259
C	GLY260
C	ASN261

site_id	BC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE FES D3001

Chain	Residue
D	CYS113
D	GLY114
D	CYS116
D	CYS148
D	ARG149
D	CYS150

site_id	BC3
Number of Residues	8
Details	BINDING SITE FOR RESIDUE FES D3002

Chain	Residue
D	GLY42
D	CYS43
D	GLY44
D	GLY46
D	CYS48
D	GLY49
D	CYS51
D	CYS73

site_id	BC4
Number of Residues	24
Details	BINDING SITE FOR RESIDUE FAD D3006

Chain	Residue
D	GLY46
D	LYS256
D	LEU257
D	VAL258
D	VAL259
D	GLY260
D	ASN261
D	THR262
D	GLU263
D	ILE264
D	ALA301
D	PHE337
D	ALA346
D	SER347
D	GLY350
D	ASN351
D	ILE353
D	THR354
D	SER359
D	ASP360
D	ILE403
D	LEU404
D	LYS422
D	ASP430

site_id	BC5
Number of Residues	9
Details	BINDING SITE FOR RESIDUE GOL A3007

Chain	Residue
A	ARG840
A	HIS841
A	ILE878
A	THR910
A	ALA911
A	PHE912
A	PHE915
A	GLY916
A	GLN919

site_id	BC6
Number of Residues	8
Details	BINDING SITE FOR RESIDUE GOL B3007

Chain	Residue
B	ARG840
B	HIS841
B	ILE878
B	THR910
B	PHE912
B	PHE915
B	GLY916
B	GLN919

site_id	BC7
Number of Residues	9
Details	BINDING SITE FOR RESIDUE GOL C3007

Chain	Residue
C	ARG840
C	HIS841
C	ILE878
C	THR910
C	ALA911
C	PHE912
C	PHE915
C	GLY916
C	GLN919

site_id	BC8
Number of Residues	9
Details	BINDING SITE FOR RESIDUE GOL D3007

Chain	Residue
D	ARG840
D	HIS841
D	ILE878
D	THR910
D	ALA911
D	PHE912
D	PHE915
D	GLY916
D	GLN919

site_id	BC9
Number of Residues	2
Details	BINDING SITE FOR RESIDUE ACY D3008

Chain	Residue
D	ALA1079
D	PO43009

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. GFggKetrstvvstava..LaayKTgrpVrCmlDRdeD

Chain	Residue	Details
A	GLY798-ASP833

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	740
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	4
Details	Active site: {"description":"Proton acceptor"}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	56
Details	Binding site: {}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	56
Details	Binding site: {"evidences":[{"source":"PubMed","id":"17301077","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"FEB-2009","submissionDatabase":"PDB data bank","title":"Human milk xanthine dehydrogenase is incompletely converted to the oxidase form in the absence of proteolysis. A structural explanation.","authors":["Pearson A.R.","Godber B.L.J.","Eisenthal R.","Taylor G.L.","Harrison R."]}}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	12
Details	Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	CSA1
Number of Residues	1
Details	Annotated By Reference To The Literature 1fiq

Chain	Residue	Details
A	GLU1262

site_id	CSA2
Number of Residues	1
Details	Annotated By Reference To The Literature 1fiq

Chain	Residue	Details
B	GLU1262

site_id	CSA3
Number of Residues	1
Details	Annotated By Reference To The Literature 1fiq

Chain	Residue	Details
C	GLU1262

site_id	CSA4
Number of Residues	1
Details	Annotated By Reference To The Literature 1fiq

Chain	Residue	Details
D	GLU1262

site_id	CSA5
Number of Residues	2
Details	Annotated By Reference To The Literature 1fiq

Chain	Residue	Details
A	GLN768
A	ARG913

site_id	CSA6
Number of Residues	2
Details	Annotated By Reference To The Literature 1fiq

Chain	Residue	Details
B	GLN768
B	ARG913

site_id	CSA7
Number of Residues	2
Details	Annotated By Reference To The Literature 1fiq

Chain	Residue	Details
C	GLN768
C	ARG913

site_id	CSA8
Number of Residues	2
Details	Annotated By Reference To The Literature 1fiq

Chain	Residue	Details
D	GLN768
D	ARG913

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)