Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2V4J

THE CRYSTAL STRUCTURE OF Desulfovibrio vulgaris DISSIMILATORY SULFITE REDUCTASE BOUND TO DsrC PROVIDES NOVEL INSIGHTS INTO THE MECHANISM OF SULFATE RESPIRATION

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000103	biological_process	sulfate assimilation
A	0005515	molecular_function	protein binding
A	0009337	cellular_component	sulfite reductase complex (NADPH)
A	0016002	molecular_function	sulfite reductase activity
A	0016491	molecular_function	oxidoreductase activity
A	0018551	molecular_function	dissimilatory sulfite reductase (NADH) activity
A	0020037	molecular_function	heme binding
A	0046872	molecular_function	metal ion binding
A	0050311	molecular_function	sulfite reductase (ferredoxin) activity
A	0051536	molecular_function	iron-sulfur cluster binding
A	0051539	molecular_function	4 iron, 4 sulfur cluster binding
B	0000103	biological_process	sulfate assimilation
B	0005515	molecular_function	protein binding
B	0006790	biological_process	sulfur compound metabolic process
B	0009055	molecular_function	electron transfer activity
B	0009337	cellular_component	sulfite reductase complex (NADPH)
B	0016002	molecular_function	sulfite reductase activity
B	0016491	molecular_function	oxidoreductase activity
B	0018551	molecular_function	dissimilatory sulfite reductase (NADH) activity
B	0020037	molecular_function	heme binding
B	0046872	molecular_function	metal ion binding
B	0050311	molecular_function	sulfite reductase (ferredoxin) activity
B	0051536	molecular_function	iron-sulfur cluster binding
B	0051539	molecular_function	4 iron, 4 sulfur cluster binding
C	0002143	biological_process	tRNA wobble position uridine thiolation
C	0005515	molecular_function	protein binding
C	0005737	cellular_component	cytoplasm
C	0016491	molecular_function	oxidoreductase activity
C	0018551	molecular_function	dissimilatory sulfite reductase (NADH) activity
C	0097163	molecular_function	sulfur carrier activity
D	0000103	biological_process	sulfate assimilation
D	0005515	molecular_function	protein binding
D	0009337	cellular_component	sulfite reductase complex (NADPH)
D	0016002	molecular_function	sulfite reductase activity
D	0016491	molecular_function	oxidoreductase activity
D	0018551	molecular_function	dissimilatory sulfite reductase (NADH) activity
D	0020037	molecular_function	heme binding
D	0046872	molecular_function	metal ion binding
D	0050311	molecular_function	sulfite reductase (ferredoxin) activity
D	0051536	molecular_function	iron-sulfur cluster binding
D	0051539	molecular_function	4 iron, 4 sulfur cluster binding
E	0000103	biological_process	sulfate assimilation
E	0005515	molecular_function	protein binding
E	0006790	biological_process	sulfur compound metabolic process
E	0009055	molecular_function	electron transfer activity
E	0009337	cellular_component	sulfite reductase complex (NADPH)
E	0016002	molecular_function	sulfite reductase activity
E	0016491	molecular_function	oxidoreductase activity
E	0018551	molecular_function	dissimilatory sulfite reductase (NADH) activity
E	0020037	molecular_function	heme binding
E	0046872	molecular_function	metal ion binding
E	0050311	molecular_function	sulfite reductase (ferredoxin) activity
E	0051536	molecular_function	iron-sulfur cluster binding
E	0051539	molecular_function	4 iron, 4 sulfur cluster binding
F	0002143	biological_process	tRNA wobble position uridine thiolation
F	0005515	molecular_function	protein binding
F	0005737	cellular_component	cytoplasm
F	0016491	molecular_function	oxidoreductase activity
F	0018551	molecular_function	dissimilatory sulfite reductase (NADH) activity
F	0097163	molecular_function	sulfur carrier activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	9
Details	BINDING SITE FOR RESIDUE SF4 A 501

Chain	Residue
A	CYS177
A	CYS183
A	PHE185
A	ALA186
A	ALA220
A	CYS221
A	ASN223
A	CYS225
A	SH0503

site_id	AC2
Number of Residues	8
Details	BINDING SITE FOR RESIDUE SF4 A 502

Chain	Residue
A	CYS284
A	CYS288
A	CYS303
A	VAL304
A	ARG305
A	CYS306
A	MET307
A	CYS309

site_id	AC3
Number of Residues	43
Details	BINDING SITE FOR RESIDUE SH0 A 503

Chain	Residue
A	CYS177
A	LEU178
A	ARG182
A	CYS183
A	GLU184
A	PHE185
A	ASN223
A	GLY224
A	CYS225
A	ASN262
A	ASN311
A	SF4501
A	HOH2135
A	HOH2161
A	HOH2303
A	HOH2304
A	HOH2305
A	HOH2306
A	HOH2307
A	HOH2308
A	HOH2309
A	HOH2310
A	HOH2311
A	HOH2312
B	HIS44
B	HIS54
B	ARG66
B	ARG94
B	THR96
B	THR97
B	ARG98
B	ASN100
B	GLU102
B	GLY134
B	GLY136
B	SER140
B	ARG183
B	LYS288
B	VAL289
B	SER290
B	ARG292
B	ARG336
B	HOH2210

site_id	AC4
Number of Residues	8
Details	BINDING SITE FOR RESIDUE SF4 B 501

Chain	Residue
B	CYS151
B	THR153
B	PRO154
B	CYS188
B	CYS189
B	ASN191
B	CYS193
B	SRM503

site_id	AC5
Number of Residues	7
Details	BINDING SITE FOR RESIDUE SF4 B 502

Chain	Residue
B	CYS231
B	VAL236
B	CYS258
B	MET259
B	CYS261
B	GLY262
B	CYS264

site_id	AC6
Number of Residues	35
Details	BINDING SITE FOR RESIDUE SRM B 503

Chain	Residue
B	HIS152
B	ASN191
B	CYS193
B	GLY194
B	SF4501
B	SO3504
B	HOH2150
B	HOH2273
B	HOH2274
C	GLY103
C	CYS104
A	ILE81
A	ARG83
A	ARG101
A	GLY134
A	SER135
A	THR136
A	GLY137
A	ASP138
A	TYR212
A	LYS213
A	LYS215
A	LYS217
A	ARG231
A	LYS332
A	ALA333
A	ILE335
A	ARG376
A	ARG378
A	HOH2079
A	HOH2103
B	ARG71
B	THR145
B	GLN146
B	HIS150

site_id	AC7
Number of Residues	7
Details	BINDING SITE FOR RESIDUE SO3 B 504

Chain	Residue
A	ARG101
A	ARG172
A	LYS213
A	LYS215
B	SRM503
C	CYS104
C	HOH2058

site_id	AC8
Number of Residues	8
Details	BINDING SITE FOR RESIDUE SF4 D 501

Chain	Residue
D	CYS177
D	CYS183
D	PHE185
D	ALA186
D	ALA220
D	CYS221
D	ASN223
D	CYS225

site_id	AC9
Number of Residues	8
Details	BINDING SITE FOR RESIDUE SF4 D 502

Chain	Residue
D	CYS284
D	CYS288
D	CYS303
D	VAL304
D	ARG305
D	CYS306
D	MET307
D	CYS309

site_id	BC1
Number of Residues	38
Details	BINDING SITE FOR RESIDUE SH0 D 503

Chain	Residue
D	CYS177
D	LEU178
D	ARG182
D	CYS183
D	GLU184
D	PHE185
D	ASN223
D	GLY224
D	CYS225
D	ASN262
D	ASN311
D	HOH2052
D	HOH2173
D	HOH2174
D	HOH2175
D	HOH2176
D	HOH2177
D	HOH2178
D	HOH2179
D	HOH2180
D	HOH2181
E	HIS44
E	HIS54
E	ARG66
E	ARG94
E	THR96
E	THR97
E	ARG98
E	ASN100
E	GLU102
E	GLY134
E	GLY136
E	SER140
E	ARG183
E	VAL289
E	SER290
E	ARG292
E	ARG336

site_id	BC2
Number of Residues	8
Details	BINDING SITE FOR RESIDUE SF4 E 501

Chain	Residue
E	CYS151
E	THR153
E	PRO154
E	CYS188
E	CYS189
E	ASN191
E	CYS193
E	SRM503

site_id	BC3
Number of Residues	8
Details	BINDING SITE FOR RESIDUE SF4 E 502

Chain	Residue
E	CYS231
E	THR233
E	VAL236
E	CYS258
E	MET259
E	CYS261
E	GLY262
E	CYS264

site_id	BC4
Number of Residues	31
Details	BINDING SITE FOR RESIDUE SRM E 503

Chain	Residue
D	ILE81
D	ARG83
D	ARG101
D	GLY134
D	SER135
D	THR136
D	GLY137
D	ASP138
D	TYR212
D	LYS213
D	LYS215
D	LYS217
D	ARG231
D	ALA333
D	ILE335
D	ARG376
D	ARG378
E	ARG71
E	THR145
E	GLN146
E	HIS150
E	HIS152
E	ASN191
E	CYS193
E	GLY194
E	SF4501
E	SO3504
E	HOH2053
E	HOH2164
F	GLY103
F	CYS104

site_id	BC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO3 E 504

Chain	Residue
D	ARG101
D	ARG172
D	LYS213
D	LYS215
E	SRM503
F	CYS104

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. CmYCGnCYtMCP

Chain	Residue	Details
B	CYS258-PRO269

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	110
Details	Domain: {"description":"4Fe-4S ferredoxin-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00711","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	30
Details	Binding site: {"evidences":[{"source":"PubMed","id":"18829451","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2V4J","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	2
Details	Binding site: {"description":"axial binding residue","evidences":[{"source":"PubMed","id":"18829451","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

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