2WJM

Lipidic sponge phase crystal structure of the photosynthetic reaction centre from Blastochloris viridis (low dose)

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	22
Details	binding site for residue HEC C 401

Chain	Residue
C	TYR56
C	ILE77
C	THR78
C	SER82
C	CYS87
C	CYS90
C	HIS91
C	LEU96
C	TYR104
C	ALA107
C	ARG108
C	LYS57
C	HOH501
C	HOH634
M	PRO313
C	ASN58
C	VAL59
C	LYS60
C	VAL61
C	LEU62
C	PHE70
C	MET74

---

site_id	AC2
Number of Residues	19
Details	binding site for residue HEC C 402

Chain	Residue
C	ILE77
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	PRO142
C	LEU289
C	ARG293
C	PRO301

---

site_id	AC3
Number of Residues	20
Details	binding site for residue HEC C 403

Chain	Residue
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	HOH521
C	HOH566
C	HOH581
C	HOH593
M	ILE189

---

site_id	AC4
Number of Residues	22
Details	binding site for residue HEC C 404

Chain	Residue
C	HIS124
C	VAL125
C	THR128
C	GLY129
C	VAL130
C	LEU240
C	PHE246
C	GLN263
C	ILE266
C	ILE271
C	MET273
C	ASP304
C	CYS305
C	CYS308
C	HIS309
C	THR313
C	LYS314
C	PRO315
C	HOH508
C	HOH534
C	HOH573
C	HOH635

---

site_id	AC5
Number of Residues	6
Details	binding site for residue DGA C 405

Chain	Residue
C	CYS1
L	SER178
L	TRP262
L	TRP265
M	BCB401
M	NS5405

---

site_id	AC6
Number of Residues	22
Details	binding site for residue BCB L 301

Chain	Residue
L	VAL177
L	PHE181
L	ILE240
L	PHE241
L	GLY244
L	THR248
L	BCB302
L	BPB303
M	TYR195
M	TYR208
M	BCB401
M	BCB402
L	MET127
L	PHE128
L	VAL157
L	ASN158
L	PHE160
L	TYR162
L	TRP167
L	HIS168
L	HIS173
L	SER176

---

site_id	AC7
Number of Residues	18
Details	binding site for residue BCB L 302

Chain	Residue
L	VAL46
L	ILE49
L	PHE128
L	PHE146
L	ILE150
L	HIS153
L	LEU154
L	VAL157
L	BCB301
L	BPB303
M	TYR195
M	GLY201
M	ILE204
M	GLY205
M	TYR208
M	GLY209
M	BCB402
M	HOH565

---

site_id	AC8
Number of Residues	18
Details	binding site for residue BPB L 303

Chain	Residue
L	ILE42
L	PHE97
L	TRP100
L	GLU104
L	VAL117
L	ALA120
L	PHE121
L	PRO124
L	TYR148
L	ALA237
L	PHE241
L	BCB301
L	BCB302
M	TYR208
M	LEU212
M	TRP250
M	ILE254
M	MQ7404

---

site_id	AC9
Number of Residues	6
Details	binding site for residue MPG L 304

Chain	Residue
L	TRP115
L	HIS116
L	LEU119
L	ARG231
L	SER238
M	HOH615

---

site_id	AD1
Number of Residues	6
Details	binding site for residue MPG L 305

Chain	Residue
L	HIS190
L	LEU193
L	SER223
L	GLY225
L	HOH461
M	MPG406

---

site_id	AD2
Number of Residues	5
Details	binding site for residue FE2 L 306

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

---

site_id	AD3
Number of Residues	20
Details	binding site for residue BCB M 401

Chain	Residue
C	DGA405
L	HIS168
L	MET174
L	VAL177
L	SER178
L	PHE181
L	VAL182
L	BCB301
L	HOH428
M	MET120
M	VAL155
M	ILE158
M	ILE177
M	TRP178
M	HIS180
M	ILE181
M	LEU184
M	BCB402
M	BPB403
M	NS5405

---

site_id	AD4
Number of Residues	21
Details	binding site for residue BCB M 402

Chain	Residue
L	TYR162
L	PHE181
L	BCB301
L	BCB302
M	ILE69
M	LEU124
M	PHE148
M	PHE154
M	VAL155
M	SER188
M	PHE194
M	TYR195
M	HIS200
M	SER203
M	ILE204
M	TYR208
M	MET275
M	ALA278
M	ILE282
M	BCB401
M	BPB403

---

site_id	AD5
Number of Residues	19
Details	binding site for residue BPB M 403

Chain	Residue
L	PHE181
L	MET185
L	LEU189
L	VAL220
M	PHE59
M	SER63
M	ILE66
M	SER123
M	LEU124
M	TRP127
M	VAL131
M	ILE144
M	ASN147
M	PHE148
M	SER271
M	MET275
M	BCB401
M	BCB402
M	NS5405

---

site_id	AD6
Number of Residues	11
Details	binding site for residue MQ7 M 404

Chain	Residue
L	TYR29
L	ARG103
L	BPB303
M	HIS217
M	THR220
M	ALA246
M	ALA247
M	TRP250
M	PHE256
M	ASN257
M	ALA258

---

site_id	AD7
Number of Residues	12
Details	binding site for residue NS5 M 405

Chain	Residue
C	DGA405
M	MET73
M	GLY117
M	THR121
M	GLY159
M	CYS160
M	TRP169
M	PHE175
M	GLY176
M	ILE177
M	BCB401
M	BPB403

---

site_id	AD8
Number of Residues	4
Details	binding site for residue MPG M 406

Chain	Residue
L	VAL220
L	GLY221
L	MPG305
M	LYS31

---

site_id	AD9
Number of Residues	7
Details	binding site for residue PO4 M 407

Chain	Residue
M	TRP23
M	TYR50
M	GLY52
M	ALA53
M	SER54
M	HOH509
M	HOH525

---

site_id	AE1
Number of Residues	5
Details	binding site for residue PO4 M 408

Chain	Residue
L	ASN199
M	HIS143
M	ARG265
M	HOH501
M	HOH505

---

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

---

site_id	SWS_FT_FI8
Number of Residues	4
Details	Binding site: {"description":"axial binding residue"}

Chain

Residue

Details

---

site_id	SWS_FT_FI9
Number of Residues	7
Details	Binding site: {}

Chain

Residue

Details

---