Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3MM6

Dissimilatory sulfite reductase cyanide complex

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000103	biological_process	sulfate assimilation
A	0009337	cellular_component	sulfite reductase complex (NADPH)
A	0016002	molecular_function	sulfite reductase activity
A	0016020	cellular_component	membrane
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	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	0016020	cellular_component	membrane
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
D	0000103	biological_process	sulfate assimilation
D	0009337	cellular_component	sulfite reductase complex (NADPH)
D	0016002	molecular_function	sulfite reductase activity
D	0016020	cellular_component	membrane
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	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	0016020	cellular_component	membrane
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

Functional Information from PDB Data

site_id	AC1
Number of Residues	34
Details	BINDING SITE FOR RESIDUE SRM A 580

Chain	Residue
A	ARG80
A	LYS213
A	LYS215
A	ARG229
A	LYS314
A	ALA315
A	PHE317
A	ARG358
A	ARG360
A	HOH553
A	CYN590
A	ARG98
A	CYN591
A	HOH607
B	ARG60
B	THR134
B	GLN135
B	HIS139
B	CYS140
B	HIS141
B	THR142
B	ASN180
A	GLY131
B	CYS182
B	GLY183
B	THR249
B	SF4585
B	HOH587
A	SER132
A	THR133
A	GLY134
A	ASP135
A	TYR210
A	LYS211

site_id	AC2
Number of Residues	8
Details	BINDING SITE FOR RESIDUE SF4 A 575

Chain	Residue
A	CYS175
A	CYS181
A	ALA184
A	GLY218
A	CYS219
A	ASN221
A	CYS223
B	SRM570

site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SF4 A 576

Chain	Residue
A	CYS266
A	CYS285
A	VAL286
A	CYS288
A	MET289
A	CYS291

site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CYN A 590

Chain	Residue
A	ARG170
A	LYS211
A	LYS213
A	SRM580

site_id	AC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CYN A 591

Chain	Residue
A	ARG98
A	THR133
A	ARG170
A	LYS213
A	HOH421
A	SRM580

site_id	AC6
Number of Residues	9
Details	BINDING SITE FOR RESIDUE SF4 B 585

Chain	Residue
A	SRM580
B	THR134
B	CYS140
B	THR142
B	PRO143
B	CYS177
B	CYS178
B	ASN180
B	CYS182

site_id	AC7
Number of Residues	7
Details	BINDING SITE FOR RESIDUE SF4 B 586

Chain	Residue
B	CYS220
B	LEU225
B	CYS241
B	MET242
B	CYS244
B	GLY245
B	CYS247

site_id	AC8
Number of Residues	36
Details	BINDING SITE FOR RESIDUE SRM B 570

Chain	Residue
B	ARG172
B	LEU272
B	SER273
B	ARG276
B	ARG319
B	HOH402
B	HOH416
B	HOH425
B	HOH429
B	HOH455
B	HOH499
A	CYS175
A	MET176
A	CYS181
A	GLU182
A	PHE183
A	ASN221
A	CYS223
A	ASN293
A	SF4575
A	HOH625
B	HIS33
B	ILE41
B	ARG43
B	ARG55
B	ARG83
B	THR85
B	SER86
B	ARG87
B	ASN89
B	GLY117
B	THR118
B	TRP119
B	ALA121
B	SER129
B	MET170

site_id	AC9
Number of Residues	27
Details	BINDING SITE FOR RESIDUE SRM D 580

Chain	Residue
D	ILE78
D	ARG80
D	ARG98
D	GLY131
D	SER132
D	THR133
D	GLY134
D	ASP135
D	TYR210
D	LYS211
D	LYS213
D	LYS215
D	ARG229
D	LYS314
D	ALA315
D	PHE317
D	ARG358
D	ARG360
D	CYN592
E	ARG60
E	THR134
E	GLN135
E	HIS139
E	HIS141
E	ASN180
E	CYS182
E	THR249

site_id	BC1
Number of Residues	8
Details	BINDING SITE FOR RESIDUE SF4 D 575

Chain	Residue
D	CYS175
D	MET176
D	CYS181
D	ALA184
D	GLY218
D	CYS219
D	ASN221
D	CYS223

site_id	BC2
Number of Residues	8
Details	BINDING SITE FOR RESIDUE SF4 D 576

Chain	Residue
D	CYS266
D	CYS285
D	VAL286
D	CYS288
D	MET289
D	CYS291
D	HOH774
D	HOH775

site_id	BC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CYN D 592

Chain	Residue
D	ARG170
D	LYS211
D	LYS213
D	SRM580

site_id	BC4
Number of Residues	8
Details	BINDING SITE FOR RESIDUE SF4 E 585

Chain	Residue
E	THR134
E	CYS140
E	THR142
E	PRO143
E	CYS177
E	CYS178
E	ASN180
E	CYS182

site_id	BC5
Number of Residues	7
Details	BINDING SITE FOR RESIDUE SF4 E 586

Chain	Residue
E	CYS220
E	LEU225
E	CYS241
E	MET242
E	CYS244
E	GLY245
E	CYS247

site_id	BC6
Number of Residues	29
Details	BINDING SITE FOR RESIDUE SRM E 570

Chain	Residue
D	CYS175
D	MET176
D	CYS181
D	GLU182
D	PHE183
D	ASN221
D	CYS223
D	ASN293
E	HIS33
E	ARG43
E	ARG55
E	ARG83
E	THR85
E	SER86
E	ARG87
E	ASN89
E	GLY117
E	THR118
E	TRP119
E	ALA121
E	SER129
E	ARG172
E	LEU272
E	SER273
E	ARG276
E	ARG319
E	HOH386
E	HOH387
E	HOH693

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	CYS241-PRO252

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	116
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	28
Details	Binding site: {"evidences":[{"source":"PubMed","id":"18495156","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20822098","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3MM5","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3MMC","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	4
Details	Binding site: {"description":"axial binding residue","evidences":[{"source":"PubMed","id":"18495156","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"20822098","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

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