Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4AC5

Lipidic sponge phase crystal structure of the Bl. viridis reaction centre solved using serial femtosecond crystallography

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	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	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	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	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	21
Details	BINDING SITE FOR RESIDUE HEM C 1333

Chain	Residue
C	TYR56
C	THR75
C	ILE77
C	THR78
C	CYS87
C	CYS90
C	HIS91
C	LEU96
C	ALA97
C	TYR104
C	ALA107
C	LYS57
C	ARG108
C	HEM1334
C	ASN58
C	VAL59
C	LYS60
C	VAL61
C	LEU62
C	PHE70
C	MET74

site_id	AC2
Number of Residues	18
Details	BINDING SITE FOR RESIDUE HEM C 1334

Chain	Residue
C	TYR89
C	TYR102
C	PRO103
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
C	ALA303
C	HEM1333

site_id	AC3
Number of Residues	23
Details	BINDING SITE FOR RESIDUE HEM C 1335

Chain	Residue
C	VAL201
C	ARG202
C	VAL203
C	VAL204
C	PHE230
C	MET233
C	MET234
C	ILE236
C	SER237
C	LEU240
C	ASN243
C	CYS244
C	CYS247
C	HIS248
C	PHE253
C	GLU254
C	ARG264
C	ALA267
C	TRP268
C	ILE271
C	ARG272
C	HEM1336
M	ILE189

site_id	AC4
Number of Residues	21
Details	BINDING SITE FOR RESIDUE HEM C 1336

Chain	Residue
C	ILE117
C	HIS124
C	VAL125
C	THR128
C	LEU194
C	PHE246
C	GLN263
C	ILE266
C	ALA267
C	GLY270
C	ILE271
C	MET273
C	VAL274
C	ASP304
C	CYS305
C	CYS308
C	HIS309
C	THR313
C	LYS314
C	PRO315
C	HEM1335

site_id	AC5
Number of Residues	20
Details	BINDING SITE FOR RESIDUE BCB L 1274

Chain	Residue
L	BPB1276
M	TYR195
M	BCB1324
M	BCB1325
L	PHE97
L	PRO124
L	MET127
L	VAL157
L	ASN158
L	PHE160
L	TRP167
L	HIS168
L	HIS173
L	SER176
L	VAL177
L	PHE241
L	GLY244
L	GLY247
L	THR248
L	BCB1275

site_id	AC6
Number of Residues	11
Details	BINDING SITE FOR RESIDUE BCB L 1275

Chain	Residue
L	PHE128
L	HIS153
L	LEU154
L	BCB1274
L	BPB1276
M	TYR195
M	GLY201
M	ILE204
M	GLY205
M	LEU212
M	BCB1325

site_id	AC7
Number of Residues	19
Details	BINDING SITE FOR RESIDUE BPB L 1276

Chain	Residue
L	PHE41
L	ILE42
L	ALA96
L	PHE97
L	TRP100
L	GLU104
L	PHE121
L	PRO124
L	TYR148
L	GLY149
L	ILE150
L	ALA237
L	PHE241
L	BCB1274
L	BCB1275
M	TYR208
M	GLY211
M	LEU212
M	TRP250

site_id	AC8
Number of Residues	11
Details	BINDING SITE FOR RESIDUE BCB M 1324

Chain	Residue
L	HIS168
L	MET174
L	VAL177
L	SER178
L	BCB1274
M	MET120
M	TRP178
M	HIS180
M	BCB1325
M	BPB1326
M	NS51329

site_id	AC9
Number of Residues	16
Details	BINDING SITE FOR RESIDUE BCB M 1325

Chain	Residue
L	PHE181
L	BCB1274
L	BCB1275
M	GLY62
M	PHE154
M	LEU184
M	TYR195
M	HIS200
M	SER203
M	ILE204
M	TYR208
M	MET275
M	ALA278
M	ILE282
M	BCB1324
M	BPB1326

site_id	BC1
Number of Residues	16
Details	BINDING SITE FOR RESIDUE BPB M 1326

Chain	Residue
L	PHE181
L	MET185
L	LEU189
M	ALA58
M	SER63
M	ILE66
M	SER123
M	LEU124
M	TRP127
M	VAL131
M	ASN147
M	PHE148
M	SER271
M	MET275
M	BCB1324
M	BCB1325

site_id	BC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE FE2 M 1327

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

site_id	BC3
Number of Residues	10
Details	BINDING SITE FOR RESIDUE MQ7 M 1328

Chain	Residue
L	TYR29
L	ARG103
M	HIS217
M	THR220
M	ALA246
M	TRP250
M	ALA258
M	THR259
M	VAL263
M	TRP266

site_id	BC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE NS5 M 1329

Chain	Residue
M	GLY117
M	MET120
M	THR121
M	PHE175
M	GLY176
M	BCB1324

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
M	ASN193-ALA219
L	ASN166-GLY192

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	146
Details	Topological domain: {"description":"Periplasmic","evidences":[{"source":"PubMed","id":"2676514","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details