Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3ETR

Crystal structure of xanthine oxidase in complex with lumazine

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
L	0005506	molecular_function	iron ion binding
L	0016491	molecular_function	oxidoreductase activity
L	0046872	molecular_function	metal ion binding
L	0051536	molecular_function	iron-sulfur cluster binding
L	0051537	molecular_function	2 iron, 2 sulfur cluster binding
M	0005506	molecular_function	iron ion binding
M	0016491	molecular_function	oxidoreductase activity
M	0050660	molecular_function	flavin adenine dinucleotide binding
M	0071949	molecular_function	FAD binding
N	0005506	molecular_function	iron ion binding
N	0016491	molecular_function	oxidoreductase activity
N	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	28
Details	BINDING SITE FOR RESIDUE FAD B 606

Chain	Residue
A	GLY46
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	LEU404
B	HOH641
B	HOH647
B	HOH652
B	HOH658
B	HOH745
B	HOH755
B	HOH756

site_id	AC4
Number of Residues	18
Details	BINDING SITE FOR RESIDUE MTE C1326

Chain	Residue
A	GLN112
A	CYS150
C	GLY796
C	GLY797
C	PHE798
C	GLY799
C	ARG912
C	MET1038
C	GLY1039
C	GLN1040
C	SER1080
C	VAL1081
C	SER1082
C	GLN1194
C	MOS1327
C	HOH1391
C	HOH1420
C	HOH1473

site_id	AC5
Number of Residues	7
Details	BINDING SITE FOR RESIDUE MOS C1327

Chain	Residue
C	GLN767
C	GLY799
C	THR1077
C	ALA1078
C	ALA1079
C	GLU1261
C	MTE1326

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

Chain	Residue
C	GLU802
C	LEU873
C	PHE914
C	PHE1009
C	THR1010
C	VAL1011
C	LEU1014
C	ALA1079

site_id	AC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CA C1328

Chain	Residue
C	HIS840
C	THR909
C	GLN918
C	HOH1660

site_id	AC8
Number of Residues	7
Details	BINDING SITE FOR RESIDUE FES L 601

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

site_id	AC9
Number of Residues	9
Details	BINDING SITE FOR RESIDUE FES L 602

Chain	Residue
L	GLY42
L	CYS43
L	GLY44
L	GLY46
L	GLY47
L	CYS48
L	GLY49
L	CYS51
L	CYS73

site_id	BC1
Number of Residues	28
Details	BINDING SITE FOR RESIDUE FAD M 606

Chain	Residue
L	GLY46
M	LYS256
M	LEU257
M	VAL258
M	VAL259
M	GLY260
M	ASN261
M	THR262
M	GLU263
M	ILE264
M	ALA301
M	PHE337
M	ALA338
M	ALA346
M	SER347
M	GLY350
M	ASN351
M	THR354
M	SER359
M	ASP360
M	ILE403
M	LEU404
M	HOH626
M	HOH629
M	HOH665
M	HOH688
M	HOH700
L	GLU45

site_id	BC2
Number of Residues	17
Details	BINDING SITE FOR RESIDUE MTE N1326

Chain	Residue
L	GLN112
L	CYS150
N	GLY796
N	GLY797
N	PHE798
N	ARG912
N	MET1038
N	GLY1039
N	GLN1040
N	SER1080
N	VAL1081
N	SER1082
N	GLN1194
N	GLU1261
N	MOS1327
N	HOH1415
N	HOH1516

site_id	BC3
Number of Residues	11
Details	BINDING SITE FOR RESIDUE MOS N1327

Chain	Residue
N	LUZ1
N	GLN767
N	GLY799
N	GLU802
N	ALA910
N	PHE911
N	ARG912
N	ALA1078
N	ALA1079
N	GLU1261
N	MTE1326

site_id	BC4
Number of Residues	9
Details	BINDING SITE FOR RESIDUE LUZ N 1

Chain	Residue
N	GLU802
N	ARG880
N	PHE914
N	PHE1009
N	THR1010
N	LEU1014
N	ALA1078
N	ALA1079
N	MOS1327

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	2
Details	ACT_SITE: Proton acceptor => ECO:0000269\|PubMed:15148401

Chain	Residue	Details
C	GLU1261
M	ASP360
M	LEU404
M	LYS422
L	CYS113
L	CYS116
L	CYS148
L	CYS150
N	GLU1261
B	SER347
B	ASP360
B	LEU404
B	LYS422
M	LEU257
M	PHE337
M	SER347

site_id	SWS_FT_FI2
Number of Residues	8
Details	BINDING: BINDING => ECO:0000269\|PubMed:12421831, ECO:0000269\|PubMed:15148401, ECO:0000269\|PubMed:19109252

Chain	Residue	Details
C	GLN767
C	PHE798
C	ARG912
C	ALA1079
N	GLN767
N	PHE798
N	ARG912
N	ALA1079

site_id	SWS_FT_FI3
Number of Residues	8
Details	BINDING:

Chain	Residue	Details
C	GLU802
C	ARG880
C	PHE914
C	THR1010
N	GLU802
N	ARG880
N	PHE914
N	THR1010

Catalytic Information from CSA

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

Chain	Residue	Details
C	GLU1261

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

Chain	Residue	Details
N	GLU1261

site_id	CSA3
Number of Residues	2
Details	Annotated By Reference To The Literature 1fiq

Chain	Residue	Details
C	ARG912
C	GLN767

site_id	CSA4
Number of Residues	2
Details	Annotated By Reference To The Literature 1fiq

Chain	Residue	Details
N	ARG912
N	GLN767

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
N	GLU802	electrostatic stabiliser, hydrogen bond acceptor
N	ARG880	electrostatic stabiliser, hydrogen bond donor
N	GLU1261	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor

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