1FIQ

CRYSTAL STRUCTURE OF XANTHINE OXIDASE FROM BOVINE MILK

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

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

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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

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site_id	AC3
Number of Residues	20
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	VAL1081
C	SER1082
C	GLN1194
C	GLU1261
C	MOS1334
C	HOH1433
C	HOH1516
C	HOH1601

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site_id	AC4
Number of Residues	10
Details	BINDING SITE FOR RESIDUE MOS C 1334

Chain	Residue
C	GLN767
C	PHE798
C	GLY799
C	PHE911
C	ARG912
C	ALA1078
C	ALA1079
C	GLU1261
C	MTE1333
C	SAL1335

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site_id	AC5
Number of Residues	9
Details	BINDING SITE FOR RESIDUE SAL C 1335

Chain	Residue
C	GLU802
C	ARG880
C	PHE914
C	SER1008
C	PHE1009
C	THR1010
C	VAL1011
C	MOS1334
C	HOH1457

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site_id	AC6
Number of Residues	24
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	LEU287
B	PHE337
B	ALA338
B	ALA346
B	SER347
B	GLY350
B	ASN351
B	ILE353
B	THR354
B	SER359
B	ASP360
B	LEU404
B	HOH714

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site_id	AC7
Number of Residues	9
Details	BINDING SITE FOR RESIDUE GOL C 1336

Chain	Residue
C	ARG839
C	HIS840
C	ILE877
C	THR909
C	ALA910
C	PHE911
C	PHE914
C	GLY915
C	GLN918

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Functional Information from PROSITE/UniProt

site_id	PS00559
Number of Residues	36
Details	MOLYBDOPTERIN_EUK Eukaryotic molybdopterin oxidoreductases signature. GFggKetrstlvsvava..LaayKTghpVrCmlDRneD

Chain	Residue	Details
C	GLY797-ASP832

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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

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: Proton acceptor => ECO:0000269|PubMed:15148401

Chain	Residue	Details
B	LEU405
B	GLN423
A	CYS148
A	CYS150
C	PRO1262
B	ALA338
B	LEU348
B	LEU361

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site_id	SWS_FT_FI2
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269|PubMed:12421831, ECO:0000269|PubMed:15148401, ECO:0000269|PubMed:19109252

Chain	Residue	Details
C	ASN768
C	GLY799
C	GLY913
C	SER1080

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site_id	SWS_FT_FI3
Number of Residues	4
Details	BINDING:

Chain	Residue	Details
C	ALA881
C	GLY915
C	VAL1011
C	THR803

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Catalytic Information from CSA

site_id	MCSA1
Number of Residues	3
Details	M-CSA 139

Chain	Residue	Details
C	THR803	electrostatic stabiliser, hydrogen bond acceptor
C	ALA881	electrostatic stabiliser, hydrogen bond donor
C	PRO1262	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor

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