Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2X5U

80 microsecond Laue diffraction snapshot from crystals of a photosynthetic reaction centre without illumination.

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	19
Details	BINDING SITE FOR RESIDUE HEM C 1333

Chain	Residue
C	TYR56
C	THR78
C	CYS87
C	CYS90
C	HIS91
C	LEU96
C	ALA97
C	TYR104
C	ALA107
C	ARG108
M	PRO313
C	LYS57
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	VAL106
C	MET110
C	LEU111
C	MET113
C	THR114
C	THR131
C	CYS132
C	CYS135
C	HIS136
C	PRO140
C	LEU141
C	LEU282
C	LEU289
C	ARG293
C	PRO301

site_id	AC3
Number of Residues	16
Details	BINDING SITE FOR RESIDUE HEM C 1335

Chain	Residue
C	ARG202
C	VAL203
C	VAL204
C	MET233
C	SER237
C	ASN243
C	CYS244
C	CYS247
C	HIS248
C	PHE253
C	ARG264
C	ALA267
C	TRP268
C	ILE271
C	ARG272
M	ILE189

site_id	AC4
Number of Residues	17
Details	BINDING SITE FOR RESIDUE HEM C 1336

Chain	Residue
C	HIS124
C	THR128
C	GLY129
C	ILE236
C	LEU240
C	GLN263
C	ILE266
C	GLY270
C	ILE271
C	MET273
C	ASP304
C	CYS305
C	CYS308
C	HIS309
C	THR313
C	LYS314
C	PRO315

site_id	AC5
Number of Residues	21
Details	BINDING SITE FOR RESIDUE BCB L 1274

Chain	Residue
L	PHE97
L	MET127
L	PHE128
L	VAL157
L	ASN158
L	PHE160
L	TYR162
L	TRP167
L	HIS168
L	HIS173
L	SER176
L	VAL177
L	PHE241
L	GLY244
L	THR248
L	BCB1275
L	BPB1276
M	TYR195
M	TYR208
M	BCB1324
M	BCB1325

site_id	AC6
Number of Residues	14
Details	BINDING SITE FOR RESIDUE BCB L 1275

Chain	Residue
M	GLY201
M	ILE204
M	GLY205
M	TYR208
M	GLY209
M	BCB1325
L	PHE128
L	PHE146
L	ILE150
L	HIS153
L	LEU154
L	BCB1274
L	BPB1276
M	TYR195

site_id	AC7
Number of Residues	17
Details	BINDING SITE FOR RESIDUE BPB L 1276

Chain	Residue
L	PHE41
L	TRP100
L	GLU104
L	VAL117
L	PHE121
L	PRO124
L	PHE146
L	GLY149
L	HIS153
L	ALA237
L	PHE241
L	BCB1274
L	BCB1275
M	TYR208
M	LEU212
M	TRP250
M	ILE254

site_id	AC8
Number of Residues	12
Details	BINDING SITE FOR RESIDUE BCB M 1324

Chain	Residue
L	MET174
L	VAL177
L	SER178
L	BCB1274
M	MET120
M	VAL155
M	ILE158
M	HIS180
M	ILE181
M	LEU184
M	BCB1325
M	BPB1326

site_id	AC9
Number of Residues	19
Details	BINDING SITE FOR RESIDUE BCB M 1325

Chain	Residue
L	TYR162
L	PHE181
L	BCB1274
L	BCB1275
M	PHE154
M	VAL155
M	LEU184
M	PHE187
M	PHE194
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	15
Details	BINDING SITE FOR RESIDUE BPB M 1326

Chain	Residue
L	PHE181
L	MET185
M	PHE59
M	SER63
M	SER123
M	LEU124
M	TRP127
M	VAL131
M	ILE144
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	TRP100
M	HIS217
M	THR220
M	ALA246
M	TRP250
M	ASN257
M	ALA258
M	VAL263
M	TRP266

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

Chain

Residue

Details