Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3GYX

Crystal structure of adenylylsulfate reductase from Desulfovibrio gigas

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000104	molecular_function	succinate dehydrogenase activity
A	0005515	molecular_function	protein binding
A	0005737	cellular_component	cytoplasm
A	0005886	cellular_component	plasma membrane
A	0009055	molecular_function	electron transfer activity
A	0009061	biological_process	anaerobic respiration
A	0009973	molecular_function	adenylyl-sulfate reductase activity
A	0016491	molecular_function	oxidoreductase activity
A	0019420	biological_process	dissimilatory sulfate reduction
A	0046982	molecular_function	protein heterodimerization activity
A	0050660	molecular_function	flavin adenine dinucleotide binding
A	0051290	biological_process	protein heterotetramerization
A	0071949	molecular_function	FAD binding
B	0005515	molecular_function	protein binding
B	0005737	cellular_component	cytoplasm
B	0019420	biological_process	dissimilatory sulfate reduction
B	0046982	molecular_function	protein heterodimerization activity
B	0051290	biological_process	protein heterotetramerization
B	0051539	molecular_function	4 iron, 4 sulfur cluster binding
C	0000104	molecular_function	succinate dehydrogenase activity
C	0005515	molecular_function	protein binding
C	0005737	cellular_component	cytoplasm
C	0005886	cellular_component	plasma membrane
C	0009055	molecular_function	electron transfer activity
C	0009061	biological_process	anaerobic respiration
C	0009973	molecular_function	adenylyl-sulfate reductase activity
C	0016491	molecular_function	oxidoreductase activity
C	0019420	biological_process	dissimilatory sulfate reduction
C	0046982	molecular_function	protein heterodimerization activity
C	0050660	molecular_function	flavin adenine dinucleotide binding
C	0051290	biological_process	protein heterotetramerization
C	0071949	molecular_function	FAD binding
D	0005515	molecular_function	protein binding
D	0005737	cellular_component	cytoplasm
D	0019420	biological_process	dissimilatory sulfate reduction
D	0046982	molecular_function	protein heterodimerization activity
D	0051290	biological_process	protein heterotetramerization
D	0051539	molecular_function	4 iron, 4 sulfur cluster binding
E	0000104	molecular_function	succinate dehydrogenase activity
E	0005515	molecular_function	protein binding
E	0005737	cellular_component	cytoplasm
E	0005886	cellular_component	plasma membrane
E	0009055	molecular_function	electron transfer activity
E	0009061	biological_process	anaerobic respiration
E	0009973	molecular_function	adenylyl-sulfate reductase activity
E	0016491	molecular_function	oxidoreductase activity
E	0019420	biological_process	dissimilatory sulfate reduction
E	0046982	molecular_function	protein heterodimerization activity
E	0050660	molecular_function	flavin adenine dinucleotide binding
E	0051290	biological_process	protein heterotetramerization
E	0071949	molecular_function	FAD binding
F	0005515	molecular_function	protein binding
F	0005737	cellular_component	cytoplasm
F	0019420	biological_process	dissimilatory sulfate reduction
F	0046982	molecular_function	protein heterodimerization activity
F	0051290	biological_process	protein heterotetramerization
F	0051539	molecular_function	4 iron, 4 sulfur cluster binding
G	0000104	molecular_function	succinate dehydrogenase activity
G	0005515	molecular_function	protein binding
G	0005737	cellular_component	cytoplasm
G	0005886	cellular_component	plasma membrane
G	0009055	molecular_function	electron transfer activity
G	0009061	biological_process	anaerobic respiration
G	0009973	molecular_function	adenylyl-sulfate reductase activity
G	0016491	molecular_function	oxidoreductase activity
G	0019420	biological_process	dissimilatory sulfate reduction
G	0046982	molecular_function	protein heterodimerization activity
G	0050660	molecular_function	flavin adenine dinucleotide binding
G	0051290	biological_process	protein heterotetramerization
G	0071949	molecular_function	FAD binding
H	0005515	molecular_function	protein binding
H	0005737	cellular_component	cytoplasm
H	0019420	biological_process	dissimilatory sulfate reduction
H	0046982	molecular_function	protein heterodimerization activity
H	0051290	biological_process	protein heterotetramerization
H	0051539	molecular_function	4 iron, 4 sulfur cluster binding
I	0000104	molecular_function	succinate dehydrogenase activity
I	0005515	molecular_function	protein binding
I	0005737	cellular_component	cytoplasm
I	0005886	cellular_component	plasma membrane
I	0009055	molecular_function	electron transfer activity
I	0009061	biological_process	anaerobic respiration
I	0009973	molecular_function	adenylyl-sulfate reductase activity
I	0016491	molecular_function	oxidoreductase activity
I	0019420	biological_process	dissimilatory sulfate reduction
I	0046982	molecular_function	protein heterodimerization activity
I	0050660	molecular_function	flavin adenine dinucleotide binding
I	0051290	biological_process	protein heterotetramerization
I	0071949	molecular_function	FAD binding
J	0005515	molecular_function	protein binding
J	0005737	cellular_component	cytoplasm
J	0019420	biological_process	dissimilatory sulfate reduction
J	0046982	molecular_function	protein heterodimerization activity
J	0051290	biological_process	protein heterotetramerization
J	0051539	molecular_function	4 iron, 4 sulfur cluster binding
K	0000104	molecular_function	succinate dehydrogenase activity
K	0005515	molecular_function	protein binding
K	0005737	cellular_component	cytoplasm
K	0005886	cellular_component	plasma membrane
K	0009055	molecular_function	electron transfer activity
K	0009061	biological_process	anaerobic respiration
K	0009973	molecular_function	adenylyl-sulfate reductase activity
K	0016491	molecular_function	oxidoreductase activity
K	0019420	biological_process	dissimilatory sulfate reduction
K	0046982	molecular_function	protein heterodimerization activity
K	0050660	molecular_function	flavin adenine dinucleotide binding
K	0051290	biological_process	protein heterotetramerization
K	0071949	molecular_function	FAD binding
L	0005515	molecular_function	protein binding
L	0005737	cellular_component	cytoplasm
L	0019420	biological_process	dissimilatory sulfate reduction
L	0046982	molecular_function	protein heterodimerization activity
L	0051290	biological_process	protein heterotetramerization
L	0051539	molecular_function	4 iron, 4 sulfur cluster binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	31
Details	BINDING SITE FOR RESIDUE FAD A 1000

Chain	Residue
A	GLY31
A	ALA69
A	VAL70
A	LEU74
A	ALA76
A	ASN78
A	PHE192
A	ILE193
A	ALA230
A	CYS231
A	GLY232
A	GLY32
A	TRP251
A	TYR252
A	PRO253
A	SER259
A	MET385
A	SER417
A	HIS418
A	ALA461
A	ASP462
A	PHE471
A	GLY33
A	SER472
A	SER475
A	MET34
A	GLY35
A	ASP60
A	LYS61
A	SER67
A	GLY68

site_id	AC2
Number of Residues	8
Details	BINDING SITE FOR RESIDUE SF4 B 1000

Chain	Residue
B	THR3
B	CYS25
B	ASN41
B	CYS47
B	GLU49
B	CYS50
B	TYR51
B	CYS53

site_id	AC3
Number of Residues	9
Details	BINDING SITE FOR RESIDUE SF4 B 2000

Chain	Residue
B	CYS10
B	ASP11
B	GLY12
B	CYS13
B	THR19
B	CYS21
B	ALA39
B	CYS57
B	ILE62

site_id	AC4
Number of Residues	27
Details	BINDING SITE FOR RESIDUE FAD C 1000

Chain	Residue
C	GLY32
C	GLY33
C	MET34
C	GLY35
C	ASP60
C	LYS61
C	SER67
C	GLY68
C	ALA69
C	LEU74
C	ALA76
C	ASN78
C	PHE192
C	ILE193
C	ALA230
C	CYS231
C	TRP251
C	TYR252
C	PRO253
C	SER259
C	SER417
C	HIS418
C	ALA461
C	ASP462
C	PHE471
C	SER472
C	SER475

site_id	AC5
Number of Residues	10
Details	BINDING SITE FOR RESIDUE SF4 D 1000

Chain	Residue
D	THR3
D	CYS25
D	PRO26
D	ASN41
D	CYS47
D	TRP48
D	GLU49
D	CYS50
D	TYR51
D	CYS53

site_id	AC6
Number of Residues	9
Details	BINDING SITE FOR RESIDUE SF4 D 2000

Chain	Residue
D	CYS10
D	ASP11
D	GLY12
D	CYS13
D	ALA20
D	CYS21
D	ALA39
D	CYS57
D	ILE62

site_id	AC7
Number of Residues	31
Details	BINDING SITE FOR RESIDUE FAD E 1000

Chain	Residue
E	ASP60
E	LYS61
E	SER67
E	GLY68
E	ALA69
E	VAL70
E	LEU74
E	ALA76
E	ILE77
E	ASN78
E	PHE192
E	ILE193
E	ALA230
E	CYS231
E	GLY232
E	TRP251
E	TYR252
E	PRO253
E	SER259
E	SER417
E	HIS418
E	ALA461
E	ASP462
E	PHE471
E	SER472
E	SER475
E	GLY31
E	GLY32
E	GLY33
E	MET34
E	GLY35

site_id	AC8
Number of Residues	9
Details	BINDING SITE FOR RESIDUE SF4 F 1000

Chain	Residue
F	THR3
F	CYS25
F	PRO26
F	MET30
F	CYS47
F	TRP48
F	CYS50
F	SER52
F	CYS53

site_id	AC9
Number of Residues	7
Details	BINDING SITE FOR RESIDUE SF4 F 2000

Chain	Residue
F	CYS10
F	CYS13
F	CYS21
F	ALA39
F	CYS57
F	PRO58
F	ILE62

site_id	BC1
Number of Residues	33
Details	BINDING SITE FOR RESIDUE FAD G 1000

Chain	Residue
G	GLY31
G	GLY32
G	GLY33
G	MET34
G	GLY35
G	ASP60
G	LYS61
G	SER67
G	GLY68
G	ALA69
G	VAL70
G	LEU74
G	ALA76
G	ILE77
G	ASN78
G	ILE191
G	PHE192
G	ILE193
G	ALA230
G	CYS231
G	GLY232
G	TRP251
G	TYR252
G	PRO253
G	SER259
G	MET385
G	SER417
G	HIS418
G	ALA461
G	ASP462
G	PHE471
G	SER472
G	SER475

site_id	BC2
Number of Residues	9
Details	BINDING SITE FOR RESIDUE SF4 H 1000

Chain	Residue
G	TRP255
H	THR3
H	CYS25
H	PRO26
H	ASN41
H	CYS47
H	CYS50
H	TYR51
H	CYS53

site_id	BC3
Number of Residues	11
Details	BINDING SITE FOR RESIDUE SF4 H 2000

Chain	Residue
H	CYS10
H	ASP11
H	GLY12
H	CYS13
H	THR19
H	ALA20
H	CYS21
H	CYS57
H	PRO58
H	GLN59
H	ILE62

site_id	BC4
Number of Residues	31
Details	BINDING SITE FOR RESIDUE FAD I 1000

Chain	Residue
I	GLY31
I	GLY32
I	GLY33
I	MET34
I	GLY35
I	ASP60
I	LYS61
I	SER67
I	GLY68
I	ALA69
I	VAL70
I	LEU74
I	ALA76
I	ASN78
I	ILE191
I	PHE192
I	ILE193
I	ALA230
I	CYS231
I	GLY232
I	TRP251
I	TYR252
I	PRO253
I	SER259
I	MET385
I	SER417
I	ALA461
I	ASP462
I	PHE471
I	SER472
I	SER475

site_id	BC5
Number of Residues	8
Details	BINDING SITE FOR RESIDUE SF4 J 1000

Chain	Residue
J	THR3
J	CYS25
J	PRO26
J	ASN41
J	CYS47
J	CYS50
J	TYR51
J	CYS53

site_id	BC6
Number of Residues	9
Details	BINDING SITE FOR RESIDUE SF4 J 2000

Chain	Residue
J	CYS10
J	ASP11
J	GLY12
J	CYS13
J	THR19
J	CYS21
J	CYS57
J	GLN59
J	ILE62

site_id	BC7
Number of Residues	28
Details	BINDING SITE FOR RESIDUE FAD K 1000

Chain	Residue
K	GLY31
K	GLY32
K	GLY33
K	MET34
K	GLY35
K	ASP60
K	LYS61
K	SER67
K	GLY68
K	ALA69
K	VAL70
K	LEU74
K	ALA76
K	ASN78
K	PHE192
K	ILE193
K	ALA230
K	CYS231
K	GLY232
K	TRP251
K	PRO253
K	SER259
K	SER417
K	ALA461
K	ASP462
K	PHE471
K	SER472
K	SER475

site_id	BC8
Number of Residues	7
Details	BINDING SITE FOR RESIDUE SF4 L 1000

Chain	Residue
L	THR3
L	CYS25
L	ASN41
L	CYS47
L	CYS50
L	TYR51
L	CYS53

site_id	BC9
Number of Residues	10
Details	BINDING SITE FOR RESIDUE SF4 L 2000

Chain	Residue
L	VAL5
L	CYS10
L	GLY12
L	CYS13
L	THR19
L	ALA20
L	CYS21
L	CYS57
L	GLN59
L	ILE62

Functional Information from PROSITE/UniProt

site_id	PS00198
Number of Residues	12
Details	4FE4S_FER_1 4Fe-4S ferredoxin-type iron-sulfur binding region signature. CwECYsCIkICP

Chain	Residue	Details
B	CYS47-PRO58

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	42
Details	Binding site: {"evidences":[{"source":"PubMed","id":"19820092","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	78
Details	Binding site: {"evidences":[{"source":"PubMed","id":"19820092","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3GYX","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	6
Details	Site: {"description":"Important for interaction with AprB and for the recognition of substrate at the substrate channel entrance","evidences":[{"source":"PubMed","id":"19820092","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	12
Details	Site: {"description":"Important for interaction with AprB and for the binding of substrate at the substrate channel entrance","evidences":[{"source":"PubMed","id":"19820092","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	174
Details	Domain: {"description":"4Fe-4S ferredoxin-type 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00711","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	6
Details	Site: {"description":"Important for the electron transfer from the iron-sulfur cluster 1 to the FAD of AprA","evidences":[{"evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	18
Details	Site: {"description":"Important for interaction with AprA at the substrate channel entrance","evidences":[{"source":"PubMed","id":"19820092","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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