Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2W54

Crystal Structure of Xanthine Dehydrogenase from Rhodobacter capsulatus in Complex with Bound Inhibitor Pterin-6-aldehyde

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0004854	molecular_function	xanthine dehydrogenase activity
A	0005506	molecular_function	iron ion binding
A	0016491	molecular_function	oxidoreductase activity
A	0046872	molecular_function	metal ion binding
A	0050660	molecular_function	flavin adenine dinucleotide binding
A	0051536	molecular_function	iron-sulfur cluster binding
A	0051537	molecular_function	2 iron, 2 sulfur cluster binding
A	0071949	molecular_function	FAD binding
B	0005506	molecular_function	iron ion binding
B	0016491	molecular_function	oxidoreductase activity
B	0030151	molecular_function	molybdenum ion binding
B	0046872	molecular_function	metal ion binding
C	0000166	molecular_function	nucleotide binding
C	0004854	molecular_function	xanthine dehydrogenase activity
C	0005506	molecular_function	iron ion binding
C	0016491	molecular_function	oxidoreductase activity
C	0046872	molecular_function	metal ion binding
C	0050660	molecular_function	flavin adenine dinucleotide binding
C	0051536	molecular_function	iron-sulfur cluster binding
C	0051537	molecular_function	2 iron, 2 sulfur cluster binding
C	0071949	molecular_function	FAD binding
D	0005506	molecular_function	iron ion binding
D	0016491	molecular_function	oxidoreductase activity
D	0030151	molecular_function	molybdenum ion binding
D	0046872	molecular_function	metal ion binding
E	0000166	molecular_function	nucleotide binding
E	0004854	molecular_function	xanthine dehydrogenase activity
E	0005506	molecular_function	iron ion binding
E	0016491	molecular_function	oxidoreductase activity
E	0046872	molecular_function	metal ion binding
E	0050660	molecular_function	flavin adenine dinucleotide binding
E	0051536	molecular_function	iron-sulfur cluster binding
E	0051537	molecular_function	2 iron, 2 sulfur cluster binding
E	0071949	molecular_function	FAD binding
F	0005506	molecular_function	iron ion binding
F	0016491	molecular_function	oxidoreductase activity
F	0030151	molecular_function	molybdenum ion binding
F	0046872	molecular_function	metal ion binding
G	0000166	molecular_function	nucleotide binding
G	0004854	molecular_function	xanthine dehydrogenase activity
G	0005506	molecular_function	iron ion binding
G	0016491	molecular_function	oxidoreductase activity
G	0046872	molecular_function	metal ion binding
G	0050660	molecular_function	flavin adenine dinucleotide binding
G	0051536	molecular_function	iron-sulfur cluster binding
G	0051537	molecular_function	2 iron, 2 sulfur cluster binding
G	0071949	molecular_function	FAD binding
H	0005506	molecular_function	iron ion binding
H	0016491	molecular_function	oxidoreductase activity
H	0030151	molecular_function	molybdenum ion binding
H	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE FES A 1463

Chain	Residue
A	GLN102
A	CYS103
A	CYS106
A	CYS134
A	ARG135
A	CYS136

site_id	AC2
Number of Residues	8
Details	BINDING SITE FOR RESIDUE FES A 1464

Chain	Residue
A	GLY42
A	CYS44
A	GLY45
A	CYS47
A	CYS63
A	GLY38
A	CYS39
A	ASN40

site_id	AC3
Number of Residues	22
Details	BINDING SITE FOR RESIDUE XAX B 1778

Chain	Residue
A	GLN102
A	CYS136
B	GLN197
B	GLY226
B	GLY227
B	PHE228
B	GLY229
B	PHE341
B	ARG342
B	MET488
B	GLY489
B	GLN490
B	ALA528
B	ALA529
B	SER530
B	SER531
B	GLY532
B	ALA533
B	GLN663
B	GLY729
B	GLU730
B	HHR1780

site_id	AC4
Number of Residues	28
Details	BINDING SITE FOR RESIDUE FAD A 1465

Chain	Residue
A	GLU41
A	GLY42
A	ASP43
A	LEU201
A	ALA203
A	GLY204
A	GLY205
A	THR206
A	ASP207
A	VAL208
A	TRP211
A	LEU225
A	PHE270
A	ALA271
A	ALA279
A	THR280
A	GLY283
A	ASN284
A	ALA286
A	ASN287
A	GLY292
A	ASP293
A	ARG330
A	PHE335
A	VAL336
A	LYS352
A	GLN359
A	ASP360

site_id	AC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE BA B 1779

Chain	Residue
B	GLU172
B	HIS173
B	TYR175
B	THR266
B	GLY267

site_id	AC6
Number of Residues	12
Details	BINDING SITE FOR RESIDUE HHR B 1780

Chain	Residue
B	GLU232
B	PRO306
B	ARG310
B	PHE344
B	PHE459
B	THR460
B	LEU461
B	LEU464
B	ALA528
B	ALA529
B	GLU730
B	XAX1778

site_id	AC7
Number of Residues	7
Details	BINDING SITE FOR RESIDUE FES C 1463

Chain	Residue
C	GLN102
C	CYS103
C	GLY104
C	CYS106
C	CYS134
C	ARG135
C	CYS136

site_id	AC8
Number of Residues	9
Details	BINDING SITE FOR RESIDUE FES C 1464

Chain	Residue
C	GLY38
C	CYS39
C	ASN40
C	GLY42
C	ASP43
C	CYS44
C	GLY45
C	CYS47
C	CYS63

site_id	AC9
Number of Residues	22
Details	BINDING SITE FOR RESIDUE XAX D 1778

Chain	Residue
D	GLN197
D	GLY226
D	GLY227
D	PHE228
D	GLY229
D	PHE341
D	ARG342
D	MET488
D	GLY489
D	GLN490
D	ALA528
D	ALA529
D	SER530
D	SER531
D	GLY532
D	ALA533
D	GLN663
D	GLY729
D	GLU730
D	HHR1780
C	GLN102
C	CYS136

site_id	BC1
Number of Residues	27
Details	BINDING SITE FOR RESIDUE FAD C 1465

Chain	Residue
C	GLU41
C	GLY42
C	LEU201
C	ALA203
C	GLY204
C	GLY205
C	THR206
C	ASP207
C	VAL208
C	TRP211
C	LEU225
C	ALA245
C	PHE270
C	ALA271
C	ALA279
C	THR280
C	GLY283
C	ASN284
C	ALA286
C	GLY292
C	ASP293
C	ARG330
C	PHE335
C	VAL336
C	LYS352
C	GLN359
C	ASP360

site_id	BC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE BA D 1779

Chain	Residue
D	GLU172
D	HIS173
D	TYR175
D	THR266
D	GLY267

site_id	BC3
Number of Residues	11
Details	BINDING SITE FOR RESIDUE HHR D 1780

Chain	Residue
D	GLU232
D	PRO306
D	ARG310
D	PHE344
D	PHE459
D	THR460
D	LEU461
D	LEU464
D	ALA529
D	GLU730
D	XAX1778

site_id	BC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE FES E 1463

Chain	Residue
E	GLN102
E	CYS103
E	CYS106
E	CYS134
E	ARG135
E	CYS136

site_id	BC5
Number of Residues	9
Details	BINDING SITE FOR RESIDUE FES E 1464

Chain	Residue
E	GLY38
E	CYS39
E	ASN40
E	GLY42
E	ASP43
E	CYS44
E	GLY45
E	CYS47
E	CYS63

site_id	BC6
Number of Residues	21
Details	BINDING SITE FOR RESIDUE XAX F 1778

Chain	Residue
E	GLN102
E	CYS136
F	GLN197
F	GLY227
F	PHE228
F	GLY229
F	PHE341
F	ARG342
F	MET488
F	GLY489
F	GLN490
F	ALA528
F	ALA529
F	SER530
F	SER531
F	GLY532
F	ALA533
F	GLN663
F	GLY729
F	GLU730
F	HHR1780

site_id	BC7
Number of Residues	28
Details	BINDING SITE FOR RESIDUE FAD E 1465

Chain	Residue
E	GLU41
E	GLY42
E	ASP43
E	LEU201
E	ALA203
E	GLY204
E	GLY205
E	THR206
E	ASP207
E	VAL208
E	TRP211
E	LEU225
E	PHE270
E	ALA271
E	ALA279
E	THR280
E	GLY283
E	ASN284
E	ALA286
E	ASN287
E	GLY292
E	ASP293
E	ARG330
E	PHE335
E	VAL336
E	LYS352
E	GLN359
E	ASP360

site_id	BC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE BA F 1779

Chain	Residue
F	GLU172
F	HIS173
F	TYR175
F	THR266
F	GLY267

site_id	BC9
Number of Residues	11
Details	BINDING SITE FOR RESIDUE HHR F 1780

Chain	Residue
F	GLU232
F	PRO306
F	ARG310
F	PHE344
F	PHE459
F	THR460
F	LEU461
F	LEU464
F	ALA529
F	GLU730
F	XAX1778

site_id	CC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE FES G 1463

Chain	Residue
G	GLN102
G	CYS103
G	CYS106
G	CYS134
G	ARG135
G	CYS136

site_id	CC2
Number of Residues	8
Details	BINDING SITE FOR RESIDUE FES G 1464

Chain	Residue
G	GLY38
G	CYS39
G	ASN40
G	GLY42
G	CYS44
G	GLY45
G	CYS47
G	CYS63

site_id	CC3
Number of Residues	21
Details	BINDING SITE FOR RESIDUE XAX H 1778

Chain	Residue
G	GLN102
G	CYS136
H	GLN197
H	GLY226
H	GLY227
H	PHE228
H	GLY229
H	PHE341
H	ARG342
H	MET488
H	GLY489
H	GLN490
H	ALA528
H	ALA529
H	SER530
H	GLY532
H	ALA533
H	GLN663
H	GLY729
H	GLU730
H	HHR1780

site_id	CC4
Number of Residues	27
Details	BINDING SITE FOR RESIDUE FAD G 1465

Chain	Residue
G	GLU41
G	GLY42
G	LEU201
G	ALA203
G	GLY204
G	GLY205
G	THR206
G	ASP207
G	VAL208
G	TRP211
G	LEU225
G	PHE270
G	ALA271
G	VAL275
G	ALA279
G	THR280
G	GLY283
G	ASN284
G	ALA286
G	ASN287
G	GLY292
G	ASP293
G	ARG330
G	VAL336
G	LYS352
G	GLN359
G	ASP360

site_id	CC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE BA H 1779

Chain	Residue
H	GLU172
H	HIS173
H	TYR175
H	THR266
H	GLY267

site_id	CC6
Number of Residues	11
Details	BINDING SITE FOR RESIDUE HHR H 1780

Chain	Residue
H	GLU232
H	PRO306
H	ARG310
H	PHE344
H	PHE459
H	THR460
H	LEU461
H	LEU464
H	ALA529
H	GLU730
H	XAX1778

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. CNEGDCGAC

Chain	Residue	Details
A	CYS39-CYS47

Catalytic Information from CSA

site_id	CSA1
Number of Residues	1
Details	Annotated By Reference To The Literature 1fiq

Chain	Residue	Details
B	GLU730

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

Chain	Residue	Details
D	GLU730

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

Chain	Residue	Details
F	GLU730

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

Chain	Residue	Details
H	GLU730

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

Chain	Residue	Details
B	ARG342
B	GLN197

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

Chain	Residue	Details
D	ARG342
D	GLN197

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

Chain	Residue	Details
F	ARG342
F	GLN197

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

Chain	Residue	Details
H	ARG342
H	GLN197

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)