Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3B9J

Structure of Xanthine Oxidase with 2-hydroxy-6-methylpurine

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
I	0005506	molecular_function	iron ion binding
I	0016491	molecular_function	oxidoreductase activity
I	0046872	molecular_function	metal ion binding
I	0051536	molecular_function	iron-sulfur cluster binding
I	0051537	molecular_function	2 iron, 2 sulfur cluster binding
J	0005506	molecular_function	iron ion binding
J	0016491	molecular_function	oxidoreductase activity
J	0050660	molecular_function	flavin adenine dinucleotide binding
J	0071949	molecular_function	FAD binding
K	0005506	molecular_function	iron ion binding
K	0016491	molecular_function	oxidoreductase activity
K	0043546	molecular_function	molybdopterin cofactor binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CA C 1

Chain	Residue
C	ILE877
C	THR909
C	GLN918

site_id	AC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE FES A 601

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

site_id	AC3
Number of Residues	9
Details	BINDING SITE FOR RESIDUE FES A 602

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

site_id	AC4
Number of Residues	16
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	ALA1079
C	SER1080
C	VAL1081
C	SER1082
C	GLN1194
C	MOS1334
C	HOH1552

site_id	AC5
Number of Residues	11
Details	BINDING SITE FOR RESIDUE MOS C 1334

Chain	Residue
C	GLN767
C	GLY799
C	GLU802
C	ALA910
C	PHE911
C	ARG912
C	ALA1078
C	ALA1079
C	GLU1261
C	MTE1333
C	2901335

site_id	AC6
Number of Residues	27
Details	BINDING SITE FOR RESIDUE FAD B 606

Chain	Residue
A	GLU45
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	ASP360
B	LEU404
B	HOH618
B	HOH620
B	HOH649
B	HOH665
B	HOH673

site_id	AC7
Number of Residues	7
Details	BINDING SITE FOR RESIDUE FES I 601

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

site_id	AC8
Number of Residues	9
Details	BINDING SITE FOR RESIDUE FES I 602

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

site_id	AC9
Number of Residues	19
Details	BINDING SITE FOR RESIDUE MTE K 1333

Chain	Residue
K	SER1080
K	VAL1081
K	SER1082
K	GLN1194
K	GLU1261
K	MOS1334
K	HOH1419
K	HOH1453
K	HOH1615
I	GLN112
I	CYS150
K	GLY797
K	PHE798
K	GLY799
K	ARG912
K	MET1038
K	GLY1039
K	GLN1040
K	ALA1079

site_id	BC1
Number of Residues	11
Details	BINDING SITE FOR RESIDUE MOS K 1334

Chain	Residue
K	GLN767
K	PHE798
K	GLY799
K	GLU802
K	PHE911
K	ARG912
K	ALA1078
K	ALA1079
K	GLU1261
K	MTE1333
K	2901335

site_id	BC2
Number of Residues	25
Details	BINDING SITE FOR RESIDUE FAD J 606

Chain	Residue
I	GLU45
I	GLY46
J	LYS256
J	LEU257
J	VAL258
J	VAL259
J	GLY260
J	ASN261
J	THR262
J	GLU263
J	ILE264
J	PHE337
J	VAL342
J	ALA346
J	SER347
J	GLY350
J	ASN351
J	ILE353
J	THR354
J	SER359
J	ASP360
J	LEU404
J	HOH629
J	HOH645
J	HOH660

site_id	BC3
Number of Residues	11
Details	BINDING SITE FOR RESIDUE 290 C 1335

Chain	Residue
C	GLU802
C	ARG880
C	PHE914
C	PHE1009
C	THR1010
C	ALA1078
C	ALA1079
C	GLU1261
C	MOS1334
C	HOH1365
C	HOH1495

site_id	BC4
Number of Residues	12
Details	BINDING SITE FOR RESIDUE 290 K 1335

Chain	Residue
K	GLU802
K	ARG880
K	PHE914
K	SER1008
K	PHE1009
K	THR1010
K	ALA1078
K	ALA1079
K	GLU1261
K	MOS1334
K	HOH1624
K	HOH1625

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
J	ASP360
J	LEU404
J	LYS422
I	CYS113
I	CYS116
I	CYS148
I	CYS150
K	GLU1261
B	SER347
B	ASP360
B	LEU404
B	LYS422
J	LEU257
J	PHE337
J	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
K	GLN767
K	PHE798
K	ARG912
K	ALA1079

site_id	SWS_FT_FI3
Number of Residues	8
Details	BINDING:

Chain	Residue	Details
C	GLU802
C	ARG880
C	PHE914
C	THR1010
K	GLU802
K	ARG880
K	PHE914
K	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
K	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
K	ARG912
K	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
K	GLU802	electrostatic stabiliser, hydrogen bond acceptor
K	ARG880	electrostatic stabiliser, hydrogen bond donor
K	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)