Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3NRZ

Crystal Structure of Bovine Xanthine Oxidase in Complex with Hypoxanthine

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005506	molecular_function	iron ion binding
A	0016491	molecular_function	oxidoreductase activity
A	0046872	molecular_function	metal ion binding
A	0051536	molecular_function	iron-sulfur cluster binding
A	0051537	molecular_function	2 iron, 2 sulfur cluster binding
B	0005506	molecular_function	iron ion binding
B	0016491	molecular_function	oxidoreductase activity
B	0050660	molecular_function	flavin adenine dinucleotide binding
B	0071949	molecular_function	FAD binding
C	0005506	molecular_function	iron ion binding
C	0016491	molecular_function	oxidoreductase activity
C	0043546	molecular_function	molybdopterin cofactor binding
J	0005506	molecular_function	iron ion binding
J	0016491	molecular_function	oxidoreductase activity
J	0046872	molecular_function	metal ion binding
J	0051536	molecular_function	iron-sulfur cluster binding
J	0051537	molecular_function	2 iron, 2 sulfur cluster binding
K	0005506	molecular_function	iron ion binding
K	0016491	molecular_function	oxidoreductase activity
K	0050660	molecular_function	flavin adenine dinucleotide binding
K	0071949	molecular_function	FAD binding
L	0005506	molecular_function	iron ion binding
L	0016491	molecular_function	oxidoreductase activity
L	0043546	molecular_function	molybdopterin cofactor binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE FES A 601

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

site_id	AC2
Number of Residues	10
Details	BINDING SITE FOR RESIDUE FES A 602

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

site_id	AC3
Number of Residues	29
Details	BINDING SITE FOR RESIDUE FAD B 606

Chain	Residue
A	GLY46
B	LYS256
B	LEU257
B	VAL258
B	VAL259
B	GLY260
B	ASN261
B	THR262
B	GLU263
B	ILE264
B	ALA301
B	PHE337
B	ALA338
B	ALA346
B	SER347
B	GLY350
B	ASN351
B	ILE353
B	THR354
B	SER359
B	ASP360
B	ILE403
B	LEU404
B	HOH680
B	HOH782
B	HOH785
B	HOH840
B	HOH1200
B	HOH1924

site_id	AC4
Number of Residues	19
Details	BINDING SITE FOR RESIDUE MTE C 1327

Chain	Residue
A	GLN112
A	CYS150
C	HOH246
C	HOH426
C	GLY796
C	GLY797
C	PHE798
C	GLY799
C	ARG912
C	MET1038
C	GLY1039
C	GLN1040
C	ALA1079
C	SER1080
C	VAL1081
C	SER1082
C	GLN1194
C	MOS1328
C	HOH1359

site_id	AC5
Number of Residues	10
Details	BINDING SITE FOR RESIDUE MOS C 1328

Chain	Residue
C	HPA1
C	GLN767
C	GLY799
C	GLU802
C	PHE911
C	ARG912
C	ALA1078
C	ALA1079
C	GLU1261
C	MTE1327

site_id	AC6
Number of Residues	8
Details	BINDING SITE FOR RESIDUE HPA C 1

Chain	Residue
C	GLU802
C	ARG880
C	PHE914
C	SER1008
C	PHE1009
C	THR1010
C	ALA1079
C	MOS1328

site_id	AC7
Number of Residues	8
Details	BINDING SITE FOR RESIDUE FES J 601

Chain	Residue
J	GLN112
J	CYS113
J	GLY114
J	CYS116
J	CYS148
J	ARG149
J	CYS150
L	LEU744

site_id	AC8
Number of Residues	10
Details	BINDING SITE FOR RESIDUE FES J 602

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

site_id	AC9
Number of Residues	27
Details	BINDING SITE FOR RESIDUE FAD K 606

Chain	Residue
J	GLU45
J	GLY46
K	LYS256
K	LEU257
K	VAL258
K	VAL259
K	GLY260
K	ASN261
K	THR262
K	GLU263
K	ILE264
K	ALA301
K	PHE337
K	ALA338
K	ALA346
K	SER347
K	GLY350
K	ASN351
K	ILE353
K	THR354
K	SER359
K	ASP360
K	ILE403
K	LEU404
K	HOH1144
K	HOH1246
K	HOH1622

site_id	BC1
Number of Residues	21
Details	BINDING SITE FOR RESIDUE MTE L 1327

Chain	Residue
J	GLN112
J	CYS150
L	GLY796
L	GLY797
L	PHE798
L	GLY799
L	ARG912
L	MET1038
L	GLY1039
L	GLN1040
L	ALA1078
L	ALA1079
L	SER1080
L	VAL1081
L	SER1082
L	GLN1194
L	MOS1328
L	HOH1329
L	HOH1351
L	HOH1520
L	HOH1919

site_id	BC2
Number of Residues	10
Details	BINDING SITE FOR RESIDUE MOS L 1328

Chain	Residue
L	HPA1
L	GLN767
L	GLY799
L	GLU802
L	PHE911
L	ARG912
L	ALA1078
L	ALA1079
L	GLU1261
L	MTE1327

site_id	BC3
Number of Residues	7
Details	BINDING SITE FOR RESIDUE HPA L 1

Chain	Residue
L	GLU802
L	ARG880
L	PHE914
L	PHE1009
L	THR1010
L	ALA1079
L	MOS1328

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. GFggKetrstlvsvava..LaayKTghpVrCmlDRneD

Chain	Residue	Details
C	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	24
Details	Binding site: {"evidences":[{"source":"PubMed","id":"12421831","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15148401","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19109252","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
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_FI4
Number of Residues	30
Details	Binding site: {"evidences":[{"source":"PubMed","id":"12421831","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15148401","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	2
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"15148401","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	8
Details	Binding site: {}

Chain

Residue

Details

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	3
Details	M-CSA 139

Chain	Residue	Details
C	GLU802	electrostatic stabiliser, hydrogen bond acceptor
C	ARG880	electrostatic stabiliser, hydrogen bond donor
C	GLU1261	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor

site_id	MCSA2
Number of Residues	3
Details	M-CSA 139

Chain

Residue

Details

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