3NS1

Crystal Structure of Bovine Xanthine Oxidase in Complex with 6-Mercaptopurine

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	9
Details	BINDING SITE FOR RESIDUE FES A 602

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

---

site_id	AC3
Number of Residues	23
Details	BINDING SITE FOR RESIDUE FAD B 606

Chain	Residue
A	GLY46
B	HOH133
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	AC4
Number of Residues	16
Details	BINDING SITE FOR RESIDUE MTE C 1326

Chain	Residue
A	GLN112
A	CYS150
C	HOH58
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	MOS1327

---

site_id	AC5
Number of Residues	10
Details	BINDING SITE FOR RESIDUE MOS C 1327

Chain	Residue
C	PM61
C	GLN767
C	PHE798
C	GLY799
C	PHE911
C	ARG912
C	ALA1078
C	ALA1079
C	GLU1261
C	MTE1326

---

site_id	AC6
Number of Residues	7
Details	BINDING SITE FOR RESIDUE PM6 C 1

Chain	Residue
C	GLU802
C	ARG880
C	PHE914
C	PHE1009
C	THR1010
C	ALA1079
C	MOS1327

---

site_id	AC7
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	AC8
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	AC9
Number of Residues	21
Details	BINDING SITE FOR RESIDUE FAD K 606

Chain	Residue
K	PHE337
K	ALA338
K	SER347
K	GLY350
K	ASN351
K	ILE353
K	THR354
K	SER359
K	ASP360
K	LEU404
J	GLY46
K	HOH136
K	LEU257
K	VAL258
K	VAL259
K	GLY260
K	ASN261
K	THR262
K	GLU263
K	ILE264
K	ALA301

---

site_id	BC1
Number of Residues	14
Details	BINDING SITE FOR RESIDUE MTE L 1326

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	MOS1327

---

site_id	BC2
Number of Residues	10
Details	BINDING SITE FOR RESIDUE MOS L 1327

Chain	Residue
L	PM61
L	GLN767
L	GLY799
L	GLU802
L	PHE911
L	ARG912
L	ALA1078
L	ALA1079
L	GLU1261
L	MTE1326

---

site_id	BC3
Number of Residues	7
Details	BINDING SITE FOR RESIDUE PM6 L 1

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

---