Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3MMC

Structure of the dissimilatory sulfite reductase from Archaeoglobus fulgidus

Replaces: 3C7B

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	31
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	GOL590
A	HOH4067
A	ARG98
A	HOH4359
B	ARG60
B	THR134
B	GLN135
B	HIS139
B	HIS141
B	THR142
B	ASN180
B	CYS182
B	GLY183
A	GLY131
B	THR249
B	SF4585
A	SER132
A	THR133
A	GLY134
A	ASP135
A	TYR210
A	LYS211

site_id	AC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE SF4 A 575

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

site_id	AC3
Number of Residues	7
Details	BINDING SITE FOR RESIDUE SF4 A 576

Chain	Residue
A	CYS266
A	THR268
A	CYS285
A	VAL286
A	CYS288
A	MET289
A	CYS291

site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL A 590

Chain	Residue
A	ARG98
A	ARG170
A	LYS211
A	LYS213
A	SRM580
A	HOH4203

site_id	AC5
Number of Residues	10
Details	BINDING SITE FOR RESIDUE SF4 B 585

Chain	Residue
A	SRM580
B	THR134
B	GLN135
B	CYS140
B	THR142
B	PRO143
B	CYS177
B	CYS178
B	ASN180
B	CYS182

site_id	AC6
Number of Residues	8
Details	BINDING SITE FOR RESIDUE SF4 B 586

Chain	Residue
B	CYS220
B	THR222
B	LEU225
B	CYS241
B	MET242
B	CYS244
B	GLY245
B	CYS247

site_id	AC7
Number of Residues	36
Details	BINDING SITE FOR RESIDUE SRM B 570

Chain	Residue
B	HOH4009
B	HOH4015
B	HOH4023
B	HOH4027
B	HOH4034
B	HOH4380
A	CYS175
A	MET176
A	CYS181
A	GLU182
A	PHE183
A	ASN221
A	ASP222
A	CYS223
A	ASN293
A	HOH4271
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
B	ARG172
B	LEU272
B	SER273
B	ARG276
B	ARG319

site_id	AC8
Number of Residues	26
Details	BINDING SITE FOR RESIDUE SRM D 580

Chain	Residue
D	ILE78
D	ARG80
D	THR96
D	GLY131
D	SER132
D	THR133
D	GLY134
D	ILE137
D	TYR210
D	LYS211
D	LYS213
D	LYS215
D	ARG229
D	ALA315
D	PRO316
D	PHE317
D	ARG358
D	ARG360
D	HOH4535
E	GLN135
E	HIS141
E	ASN180
E	MET181
E	CYS182
E	GLY183
E	SF4585

site_id	AC9
Number of Residues	10
Details	BINDING SITE FOR RESIDUE SF4 D 575

Chain	Residue
D	CYS175
D	CYS181
D	PHE183
D	ALA184
D	GLY218
D	CYS219
D	ASN221
D	ASP222
D	CYS223
E	HOH4464

site_id	BC1
Number of Residues	8
Details	BINDING SITE FOR RESIDUE SF4 D 576

Chain	Residue
D	CYS266
D	PRO267
D	CYS285
D	VAL286
D	ARG287
D	CYS288
D	MET289
D	CYS291

site_id	BC2
Number of Residues	9
Details	BINDING SITE FOR RESIDUE SF4 E 585

Chain	Residue
D	SRM580
D	HOH4535
E	THR134
E	GLN135
E	CYS140
E	PRO143
E	CYS177
E	CYS178
E	CYS182

site_id	BC3
Number of Residues	8
Details	BINDING SITE FOR RESIDUE SF4 E 586

Chain	Residue
E	CYS220
E	THR222
E	LEU225
E	CYS241
E	TYR243
E	CYS244
E	GLY245
E	CYS247

site_id	BC4
Number of Residues	27
Details	BINDING SITE FOR RESIDUE SRM E 570

Chain	Residue
D	MET176
D	CYS181
D	GLU182
D	PHE183
D	ASN221
D	CYS223
E	HIS33
E	ILE41
E	ARG43
E	VAL53
E	ARG55
E	ARG83
E	THR85
E	SER86
E	ARG87
E	ASN89
E	GLU91
E	TRP119
E	ALA121
E	SER129
E	MET170
E	ARG172
E	LEU272
E	SER273
E	ARG276
E	ARG319
E	HOH4464

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	14
Details	BINDING: BINDING => ECO:0000269\|PubMed:18495156, ECO:0000269\|PubMed:20822098, ECO:0007744\|PDB:3MM5, ECO:0007744\|PDB:3MMC

Chain	Residue	Details
B	CYS140
E	CYS178
E	CYS220
E	CYS241
E	CYS244
E	CYS247
B	CYS177
B	CYS178
B	CYS220
B	CYS241
B	CYS244
B	CYS247
E	CYS140
E	CYS177

site_id	SWS_FT_FI2
Number of Residues	2
Details	BINDING: axial binding residue => ECO:0000305\|PubMed:18495156, ECO:0000305\|PubMed:20822098

Chain	Residue	Details
B	CYS182
E	CYS182

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