3NVY

Crystal Structure of Bovine Xanthine Oxidase in Complex with Quercetin

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	HOH560
B	HOH561
B	HOH628
B	HOH691
B	HOH1231
B	HOH1472

---

site_id	AC4
Number of Residues	21
Details	BINDING SITE FOR RESIDUE MTE C 1327

Chain	Residue
A	GLN112
A	CYS150
C	HOH96
C	HOH336
C	HOH356
C	GLY796
C	GLY797
C	PHE798
C	GLY799
C	ARG912
C	MET1038
C	GLY1039
C	GLN1040
C	ALA1078
C	ALA1079
C	SER1080
C	VAL1081
C	SER1082
C	GLN1194
C	GLU1261
C	MOS1328

---

site_id	AC5
Number of Residues	9
Details	BINDING SITE FOR RESIDUE MOS C 1328

Chain	Residue
C	GLN767
C	GLY799
C	PHE911
C	ARG912
C	ALA1078
C	ALA1079
C	GLU1261
C	MTE1327
C	QUE1356

---

site_id	AC6
Number of Residues	14
Details	BINDING SITE FOR RESIDUE QUE C 1356

Chain	Residue
C	LEU648
C	GLU802
C	LEU873
C	SER876
C	ARG880
C	PHE914
C	PHE1009
C	THR1010
C	VAL1011
C	LEU1014
C	PRO1076
C	ALA1078
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	9
Details	BINDING SITE FOR RESIDUE FES J 602

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

---

site_id	AC9
Number of Residues	26
Details	BINDING SITE FOR RESIDUE FAD K 606

Chain	Residue
J	GLY46
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	HOH531
K	HOH543
K	HOH1147
K	HOH1453

---

site_id	BC1
Number of Residues	18
Details	BINDING SITE FOR RESIDUE MTE L 1327

Chain	Residue
J	GLN112
J	CYS150
L	HOH338
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	GLU1261
L	MOS1328

---

site_id	BC2
Number of Residues	9
Details	BINDING SITE FOR RESIDUE MOS L 1328

Chain	Residue
L	GLN767
L	GLY799
L	PHE911
L	ARG912
L	ALA1078
L	ALA1079
L	GLU1261
L	MTE1327
L	QUE1356

---

site_id	BC3
Number of Residues	15
Details	BINDING SITE FOR RESIDUE QUE L 1356

Chain	Residue
L	HOH452
L	LEU648
L	GLU802
L	LEU873
L	SER876
L	ARG880
L	PHE914
L	SER1008
L	PHE1009
L	THR1010
L	VAL1011
L	LEU1014
L	ALA1078
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	2
Details	ACT_SITE: Proton acceptor => ECO:0000269|PubMed:15148401

Chain	Residue	Details
C	GLU1261
K	ASP360
K	LEU404
K	LYS422
J	CYS113
J	CYS116
J	CYS148
J	CYS150
L	GLU1261
B	SER347
B	ASP360
B	LEU404
B	LYS422
K	LEU257
K	PHE337
K	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
L	GLN767
L	PHE798
L	ARG912
L	ALA1079

---

site_id	SWS_FT_FI3
Number of Residues	8
Details	BINDING:

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

---

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
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

---