Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1DXR

Photosynthetic reaction center from Rhodopseudomonas viridis - His L168 Phe mutant (terbutryn complex)

Functional Information from GO Data

Chain	GOid	namespace	contents
C	0005506	molecular_function	iron ion binding
C	0009055	molecular_function	electron transfer activity
C	0015979	biological_process	photosynthesis
C	0016020	cellular_component	membrane
C	0019684	biological_process	photosynthesis, light reaction
C	0020037	molecular_function	heme binding
C	0030077	cellular_component	plasma membrane light-harvesting complex
C	0042717	cellular_component	plasma membrane-derived chromatophore membrane
C	0046872	molecular_function	metal ion binding
H	0015979	biological_process	photosynthesis
H	0016020	cellular_component	membrane
H	0016168	molecular_function	chlorophyll binding
H	0019684	biological_process	photosynthesis, light reaction
H	0030077	cellular_component	plasma membrane light-harvesting complex
H	0042314	molecular_function	bacteriochlorophyll binding
H	0042717	cellular_component	plasma membrane-derived chromatophore membrane
L	0009772	biological_process	photosynthetic electron transport in photosystem II
L	0015979	biological_process	photosynthesis
L	0016020	cellular_component	membrane
L	0016168	molecular_function	chlorophyll binding
L	0019684	biological_process	photosynthesis, light reaction
L	0030077	cellular_component	plasma membrane light-harvesting complex
L	0042314	molecular_function	bacteriochlorophyll binding
L	0042717	cellular_component	plasma membrane-derived chromatophore membrane
L	0046872	molecular_function	metal ion binding
M	0009772	biological_process	photosynthetic electron transport in photosystem II
M	0015979	biological_process	photosynthesis
M	0016020	cellular_component	membrane
M	0016168	molecular_function	chlorophyll binding
M	0019684	biological_process	photosynthesis, light reaction
M	0030077	cellular_component	plasma membrane light-harvesting complex
M	0042314	molecular_function	bacteriochlorophyll binding
M	0042717	cellular_component	plasma membrane-derived chromatophore membrane
M	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	20
Details	BINDING SITE FOR RESIDUE HEC C 401

Chain	Residue
C	TYR56
C	THR78
C	SER82
C	CYS87
C	CYS90
C	HIS91
C	LEU96
C	ALA97
C	TYR104
C	ALA107
C	ARG108
C	LYS57
C	VAL212
C	ASN58
C	VAL59
C	LYS60
C	VAL61
C	LEU62
C	PHE70
C	MET74

site_id	AC2
Number of Residues	16
Details	BINDING SITE FOR RESIDUE HEC C 402

Chain	Residue
C	TYR89
C	TYR102
C	VAL106
C	MET110
C	LEU111
C	MET113
C	THR114
C	CYS132
C	CYS135
C	HIS136
C	PRO140
C	LEU141
C	PRO142
C	LEU289
C	ARG293
C	PRO301

site_id	AC3
Number of Residues	22
Details	BINDING SITE FOR RESIDUE HEC C 403

Chain	Residue
C	VAL201
C	ARG202
C	VAL203
C	VAL204
C	MET233
C	SER237
C	ASN243
C	CYS244
C	CYS247
C	HIS248
C	PHE253
C	GLU254
C	ARG264
C	ALA267
C	TRP268
C	ARG272
C	HOH2148
C	HOH2214
C	HOH2215
C	HOH2216
L	TYR162
M	ILE189

site_id	AC4
Number of Residues	24
Details	BINDING SITE FOR RESIDUE HEC C 404

Chain	Residue
C	HIS124
C	VAL125
C	THR128
C	GLY129
C	LEU240
C	PHE246
C	GLN263
C	ILE266
C	ILE271
C	MET273
C	VAL274
C	ASP304
C	CYS305
C	CYS308
C	HIS309
C	THR313
C	LYS314
C	PRO315
C	HOH2217
C	HOH2218
C	HOH2219
C	HOH2220
C	HOH2221
C	HOH2222

site_id	AC5
Number of Residues	2
Details	BINDING SITE FOR RESIDUE LDA H 1259

Chain	Residue
H	ARG33
H	ASP56

site_id	AC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE LDA H 1260

Chain	Residue
H	VAL59
H	TYR60
H	LEU62
H	PRO65
H	PRO79

site_id	AC7
Number of Residues	8
Details	BINDING SITE FOR RESIDUE SO4 H 1261

Chain	Residue
H	ARG33
H	ARG37
H	TYR41
H	LEU43
H	HOH2015
H	HOH2034
H	HOH3004
M	ARG251

site_id	AC8
Number of Residues	17
Details	BINDING SITE FOR RESIDUE BCB L 400

Chain	Residue
L	VAL157
L	PHE160
L	TRP167
L	PHE168
L	HIS173
L	SER176
L	LEU180
L	ILE240
L	PHE241
L	GLY244
L	THR248
L	BCB401
M	TYR195
M	TYR208
M	BCB401
L	MET127
L	PHE128

site_id	AC9
Number of Residues	17
Details	BINDING SITE FOR RESIDUE BCB L 401

Chain	Residue
L	PHE128
L	PHE146
L	ILE150
L	HIS153
L	LEU154
L	VAL157
L	BCB400
L	BPB402
M	TYR195
M	GLY201
M	ILE204
M	GLY205
M	TYR208
M	GLY209
M	BCB401
M	LDA1325
M	HOH2077

site_id	BC1
Number of Residues	15
Details	BINDING SITE FOR RESIDUE BPB L 402

Chain	Residue
L	PHE97
L	TRP100
L	GLU104
L	VAL117
L	PHE121
L	PRO124
L	TYR148
L	HIS153
L	ALA237
L	PHE241
L	BCB401
L	MQ9501
M	TYR208
M	LEU212
M	TRP250

site_id	BC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE FE2 L 500

Chain	Residue
L	HIS190
L	HIS230
M	HIS217
M	GLU232
M	HIS264

site_id	BC3
Number of Residues	12
Details	BINDING SITE FOR RESIDUE MQ9 L 501

Chain	Residue
L	TYR29
L	PHE43
L	TRP100
L	BPB402
M	HIS217
M	THR220
M	ALA246
M	TRP250
M	PHE256
M	ALA258
M	THR259
M	VAL263

site_id	BC4
Number of Residues	11
Details	BINDING SITE FOR RESIDUE MST L 502

Chain	Residue
L	LEU189
L	HIS190
L	GLU212
L	ASN213
L	PHE216
L	TYR222
L	SER223
L	ILE224
L	GLY225
L	ILE229
L	HOH2059

site_id	BC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE LDA L 1274

Chain	Residue
L	ASP60
L	PHE62
M	TYR195
M	ALA301

site_id	BC6
Number of Residues	20
Details	BINDING SITE FOR RESIDUE BCB M 400

Chain	Residue
L	PHE168
L	MET174
L	VAL177
L	SER178
L	PHE181
L	VAL182
L	MET185
L	VAL220
L	HOH2057
M	MET120
M	VAL155
M	ILE158
M	ILE177
M	TRP178
M	HIS180
M	ILE181
M	LEU184
M	BCB401
M	BPB402
M	NS5600

site_id	BC7
Number of Residues	24
Details	BINDING SITE FOR RESIDUE BCB M 401

Chain	Residue
L	VAL157
L	TYR162
L	PHE181
L	BCB400
L	BCB401
M	GLY62
M	ILE69
M	MET120
M	PHE148
M	PHE154
M	VAL155
M	LEU184
M	SER188
M	PHE194
M	TYR195
M	HIS200
M	SER203
M	ILE204
M	TYR208
M	MET275
M	ALA278
M	ILE282
M	BCB400
M	BPB402

site_id	BC8
Number of Residues	17
Details	BINDING SITE FOR RESIDUE BPB M 402

Chain	Residue
L	PHE181
L	MET185
L	LEU189
L	VAL220
M	ALA58
M	PHE59
M	ILE66
M	SER123
M	LEU124
M	TRP127
M	VAL131
M	ILE144
M	ASN147
M	PHE148
M	SER271
M	BCB400
M	BCB401

site_id	BC9
Number of Residues	7
Details	BINDING SITE FOR RESIDUE NS5 M 600

Chain	Residue
M	GLY117
M	THR121
M	GLY159
M	CYS160
M	VAL173
M	GLY176
M	BCB400

site_id	CC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE LDA M 1324

Chain	Residue
M	TRP23
M	SER133
M	SO41329

site_id	CC2
Number of Residues	1
Details	BINDING SITE FOR RESIDUE LDA M 1325

Chain	Residue
L	BCB401

site_id	CC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE LDA M 1326

Chain	Residue
M	PHE71
M	ASN72
M	TRP112

site_id	CC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 M 1327

Chain	Residue
H	HOH2014
L	ASN199
L	HOH2062
M	HIS143
M	ARG265
M	HOH3005

site_id	CC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 M 1328

Chain	Residue
H	LEU246
H	HOH3008
L	HOH3006
M	ALA1
M	ARG226
M	HOH3007

site_id	CC6
Number of Residues	8
Details	BINDING SITE FOR RESIDUE SO4 M 1329

Chain	Residue
M	TRP23
M	TYR50
M	ALA53
M	SER54
M	SER133
M	LDA1324
M	HOH2059
M	HOH3009

Functional Information from PROSITE/UniProt

site_id	PS00244
Number of Residues	27
Details	REACTION_CENTER Photosynthetic reaction center proteins signature. NwfynPgHmsSvsflfvnamalGlHGG

Chain	Residue	Details
L	ASN166-GLY192
M	ASN193-ALA219

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	8
Details	Binding site: {"description":"axial binding residue","evidences":[{"source":"PubMed","id":"22054235","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3T6E","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	8
Details	Binding site: {"description":"covalent","evidences":[{"source":"PubMed","id":"22054235","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3T6E","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	1
Details	Site: {"description":"Not N-palmitoylated","evidences":[{"source":"PubMed","id":"22054235","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"journal article","publicationDate":"1987","firstPage":"2909","lastPage":"2914","volume":"26","journal":"Biochemistry","title":"The cytochrome subunit of the photosynthetic reaction center from Rhodopseudomonas viridis is a lipoprotein.","authors":["Weyer K.A.","Schaefer W.","Lottspeich F.","Michel H."]}},{"source":"PDB","id":"3T6E","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	1
Details	Lipidation: {"description":"S-diacylglycerol cysteine","evidences":[{"source":"PROSITE-ProRule","id":"PRU00303","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"22054235","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"journal article","publicationDate":"1987","firstPage":"2909","lastPage":"2914","volume":"26","journal":"Biochemistry","title":"The cytochrome subunit of the photosynthetic reaction center from Rhodopseudomonas viridis is a lipoprotein.","authors":["Weyer K.A.","Schaefer W.","Lottspeich F.","Michel H."]}},{"source":"PDB","id":"3T6E","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	260
Details	Transmembrane: {"description":"Helical"}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	147
Details	Topological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"2676514","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	185
Details	Topological domain: {"description":"Periplasmic","evidences":[{"source":"PubMed","id":"2676514","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details