Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3EUB

Crystal Structure of Desulfo-Xanthine Oxidase with Xanthine

Functional Information from GO Data

Chain	GOid	namespace	contents
2	0005506	molecular_function	iron ion binding
2	0016491	molecular_function	oxidoreductase activity
2	0046872	molecular_function	metal ion binding
2	0051536	molecular_function	iron-sulfur cluster binding
2	0051537	molecular_function	2 iron, 2 sulfur cluster binding
3	0005506	molecular_function	iron ion binding
3	0016491	molecular_function	oxidoreductase activity
3	0050660	molecular_function	flavin adenine dinucleotide binding
3	0071949	molecular_function	FAD binding
4	0005506	molecular_function	iron ion binding
4	0016491	molecular_function	oxidoreductase activity
4	0043546	molecular_function	molybdopterin cofactor binding
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
S	0005506	molecular_function	iron ion binding
S	0016491	molecular_function	oxidoreductase activity
S	0046872	molecular_function	metal ion binding
S	0051536	molecular_function	iron-sulfur cluster binding
S	0051537	molecular_function	2 iron, 2 sulfur cluster binding
T	0005506	molecular_function	iron ion binding
T	0016491	molecular_function	oxidoreductase activity
T	0050660	molecular_function	flavin adenine dinucleotide binding
T	0071949	molecular_function	FAD binding
U	0005506	molecular_function	iron ion binding
U	0016491	molecular_function	oxidoreductase activity
U	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	15
Details	BINDING SITE FOR RESIDUE MTE C 1333

Chain	Residue
A	GLN112
A	CYS150
C	GLY796
C	GLY797
C	PHE798
C	ARG912
C	MET1038
C	GLY1039
C	GLN1040
C	ALA1078
C	ALA1079
C	SER1080
C	SER1082
C	GLN1194
C	MOM1334

site_id	AC4
Number of Residues	11
Details	BINDING SITE FOR RESIDUE MOM C 1334

Chain	Residue
C	GLN767
C	PHE798
C	GLY799
C	GLU802
C	PHE911
C	ARG912
C	ALA1078
C	ALA1079
C	GLU1261
C	MTE1333
C	XAN7319

site_id	AC5
Number of Residues	22
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	LEU404

site_id	AC6
Number of Residues	7
Details	BINDING SITE FOR RESIDUE FES J 601

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

site_id	AC7
Number of Residues	9
Details	BINDING SITE FOR RESIDUE FES J 602

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

site_id	AC8
Number of Residues	15
Details	BINDING SITE FOR RESIDUE MTE L 1333

Chain	Residue
J	GLN112
J	CYS150
L	GLY797
L	PHE798
L	ARG912
L	MET1038
L	GLY1039
L	GLN1040
L	ALA1079
L	SER1080
L	VAL1081
L	SER1082
L	GLN1194
L	GLU1261
L	MOM1334

site_id	AC9
Number of Residues	10
Details	BINDING SITE FOR RESIDUE MOM L 1334

Chain	Residue
L	PHE911
L	ARG912
L	ALA1078
L	ALA1079
L	GLU1261
L	MTE1333
L	XAN7319
L	GLN767
L	GLY799
L	ALA910

site_id	BC1
Number of Residues	22
Details	BINDING SITE FOR RESIDUE FAD K 606

Chain	Residue
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	VAL342
K	ALA346
K	SER347
K	GLY350
K	ASN351
K	ILE353
K	SER359
K	ASP360
K	LEU404

site_id	BC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE FES S 601

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

site_id	BC3
Number of Residues	9
Details	BINDING SITE FOR RESIDUE FES S 602

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

site_id	BC4
Number of Residues	16
Details	BINDING SITE FOR RESIDUE MTE U 1333

Chain	Residue
S	GLN112
S	CYS150
U	GLY796
U	GLY797
U	PHE798
U	ARG912
U	MET1038
U	GLY1039
U	GLN1040
U	ALA1078
U	ALA1079
U	SER1080
U	VAL1081
U	SER1082
U	GLN1194
U	MOM1334

site_id	BC5
Number of Residues	9
Details	BINDING SITE FOR RESIDUE MOM U 1334

Chain	Residue
U	GLY799
U	GLU802
U	PHE911
U	ARG912
U	ALA1078
U	ALA1079
U	GLU1261
U	MTE1333
U	XAN7319

site_id	BC6
Number of Residues	23
Details	BINDING SITE FOR RESIDUE FAD T 606

Chain	Residue
S	GLY46
T	LYS256
T	LEU257
T	VAL258
T	VAL259
T	GLY260
T	ASN261
T	THR262
T	GLU263
T	ILE264
T	ALA301
T	PHE337
T	ALA338
T	ALA346
T	SER347
T	GLY350
T	ASN351
T	ILE353
T	THR354
T	SER359
T	ASP360
T	ILE403
T	LEU404

site_id	BC7
Number of Residues	7
Details	BINDING SITE FOR RESIDUE FES 2 601

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

site_id	BC8
Number of Residues	9
Details	BINDING SITE FOR RESIDUE FES 2 602

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

site_id	BC9
Number of Residues	16
Details	BINDING SITE FOR RESIDUE MTE 4 1333

Chain	Residue
2	GLN112
2	CYS150
4	GLY796
4	GLY797
4	PHE798
4	ARG912
4	MET1038
4	GLY1039
4	GLN1040
4	ALA1078
4	ALA1079
4	SER1080
4	VAL1081
4	SER1082
4	GLN1194
4	MOM1334

site_id	CC1
Number of Residues	10
Details	BINDING SITE FOR RESIDUE MOM 4 1334

Chain	Residue
4	GLN767
4	GLY799
4	GLU802
4	PHE911
4	ARG912
4	ALA1078
4	ALA1079
4	GLU1261
4	MTE1333
4	XAN7319

site_id	CC2
Number of Residues	22
Details	BINDING SITE FOR RESIDUE FAD 3 606

Chain	Residue
2	GLU45
2	GLY46
3	LYS256
3	LEU257
3	VAL258
3	VAL259
3	GLY260
3	ASN261
3	THR262
3	GLU263
3	ILE264
3	ALA301
3	PHE337
3	ALA338
3	ALA346
3	SER347
3	GLY350
3	ASN351
3	ILE353
3	THR354
3	ASP360
3	LEU404

site_id	CC3
Number of Residues	10
Details	BINDING SITE FOR RESIDUE XAN U 7319

Chain	Residue
U	GLU802
U	ARG880
U	PHE914
U	SER1008
U	PHE1009
U	THR1010
U	LEU1014
U	ALA1079
U	GLU1261
U	MOM1334

site_id	CC4
Number of Residues	9
Details	BINDING SITE FOR RESIDUE XAN C 7319

Chain	Residue
C	GLU802
C	SER876
C	ARG880
C	PHE914
C	SER1008
C	PHE1009
C	THR1010
C	ALA1079
C	MOM1334

site_id	CC5
Number of Residues	8
Details	BINDING SITE FOR RESIDUE XAN L 7319

Chain	Residue
L	GLU802
L	ARG880
L	PHE914
L	PHE1009
L	THR1010
L	LEU1014
L	ALA1079
L	MOM1334

site_id	CC6
Number of Residues	9
Details	BINDING SITE FOR RESIDUE XAN 4 7319

Chain	Residue
4	GLU802
4	SER876
4	ARG880
4	PHE914
4	PHE1009
4	THR1010
4	LEU1014
4	ALA1079
4	MOM1334

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	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	48
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	740
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	60
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	4
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	16
Details	Binding site: {}

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
C	GLU1261

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

Chain	Residue	Details
L	GLU1261

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

Chain	Residue	Details
U	GLU1261

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

Chain	Residue	Details
4	GLU1261

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

Chain	Residue	Details
C	ARG912
C	GLN767

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

Chain	Residue	Details
L	ARG912
L	GLN767

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

Chain	Residue	Details
U	ARG912
U	GLN767

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

Chain	Residue	Details
4	ARG912
4	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

site_id	MCSA3
Number of Residues	3
Details	M-CSA 139

Chain

Residue

Details

site_id	MCSA4
Number of Residues	3
Details	M-CSA 139

Chain	Residue	Details
L	GLU802	electrostatic stabiliser, hydrogen bond acceptor
L	ARG880	electrostatic stabiliser, hydrogen bond donor
L	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)