Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1PRC

CRYSTALLOGRAPHIC REFINEMENT AT 2.3 ANGSTROMS RESOLUTION AND REFINED MODEL OF THE PHOTOSYNTHETIC REACTION CENTER FROM RHODOPSEUDOMONAS VIRIDIS

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	5
Details	BINDING SITE FOR RESIDUE FE M 607

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

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 H 617

Chain	Residue
M	ARG251
H	ARG33
H	ARG37
H	TYR41
H	HOH659

site_id	AC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 M 618

Chain	Residue
L	ASN199
M	HIS143
M	ARG265

site_id	AC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 M 619

Chain	Residue
H	LEU246
M	ALA1
M	ARG226

site_id	AC5
Number of Residues	7
Details	BINDING SITE FOR RESIDUE SO4 M 620

Chain	Residue
M	TRP23
M	TYR50
M	ALA53
M	SER54
M	SER133
M	HOH666
M	HOH676

site_id	AC6
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 M 621

Chain	Residue
M	SER35
M	TYR36
M	TRP37

site_id	AC7
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 H 622

Chain	Residue
H	TYR117
H	ARG233
H	LYS237

site_id	AC8
Number of Residues	2
Details	BINDING SITE FOR RESIDUE SO4 H 623

Chain	Residue
H	ARG34
H	ARG34

site_id	AC9
Number of Residues	15
Details	BINDING SITE FOR RESIDUE BCB M 601

Chain	Residue
L	HIS168
L	MET174
L	SER178
L	PHE181
L	VAL182
L	MET185
L	HOH635
M	MET120
M	VAL155
M	TRP178
M	HIS180
M	ILE181
M	BCB603
M	BPB605
M	NS1613

site_id	BC1
Number of Residues	19
Details	BINDING SITE FOR RESIDUE BCB L 602

Chain	Residue
L	PHE97
L	PRO124
L	MET127
L	VAL157
L	PHE160
L	TRP167
L	HIS168
L	HIS173
L	SER176
L	VAL177
L	PHE241
L	GLY244
L	THR248
L	BCB604
L	BPB606
M	TYR195
M	TYR208
M	BCB603
M	MQ7608

site_id	BC2
Number of Residues	20
Details	BINDING SITE FOR RESIDUE BCB M 603

Chain	Residue
L	TYR162
L	PHE181
L	BCB602
L	BCB604
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	BCB601
M	BPB605

site_id	BC3
Number of Residues	13
Details	BINDING SITE FOR RESIDUE BCB L 604

Chain	Residue
L	PHE146
L	ILE150
L	HIS153
L	BCB602
L	BPB606
M	GLY201
M	ILE204
M	GLY205
M	TYR208
M	GLY209
M	BCB603
M	MQ7608
M	HOH645

site_id	BC4
Number of Residues	14
Details	BINDING SITE FOR RESIDUE BPB M 605

Chain	Residue
L	MET185
L	LEU189
L	VAL220
M	ILE66
M	SER123
M	LEU124
M	TRP127
M	ILE144
M	PHE148
M	SER271
M	MET275
M	BCB601
M	BCB603
L	PHE181

site_id	BC5
Number of Residues	14
Details	BINDING SITE FOR RESIDUE BPB L 606

Chain	Residue
L	PHE97
L	TRP100
L	GLU104
L	PHE121
L	PRO124
L	TYR148
L	HIS153
L	ALA237
L	PHE241
L	BCB602
L	BCB604
M	TYR208
M	LEU212
M	TRP250

site_id	BC6
Number of Residues	9
Details	BINDING SITE FOR RESIDUE MQ7 M 608

Chain	Residue
L	TYR29
L	BCB602
L	BCB604
M	ALA216
M	HIS217
M	THR220
M	TRP250
M	ALA258
M	THR259

site_id	BC7
Number of Residues	21
Details	BINDING SITE FOR RESIDUE HEC C 609

Chain	Residue
C	TYR56
C	LYS57
C	ASN58
C	VAL59
C	LYS60
C	VAL61
C	LEU62
C	PHE70
C	MET74
C	ILE77
C	THR78
C	SER82
C	CYS87
C	CYS90
C	HIS91
C	LEU96
C	ALA97
C	TYR104
C	ALA107
C	ARG108
C	VAL212

site_id	BC8
Number of Residues	16
Details	BINDING SITE FOR RESIDUE HEC C 610

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	BC9
Number of Residues	22
Details	BINDING SITE FOR RESIDUE HEC C 611

Chain	Residue
C	VAL201
C	ARG202
C	VAL203
C	VAL204
C	MET233
C	SER237
C	THR242
C	ASN243
C	CYS244
C	CYS247
C	HIS248
C	PHE253
C	GLU254
C	ARG264
C	ALA267
C	TRP268
C	ARG272
C	HOH638
C	HOH639
C	HOH640
C	HOH666
M	ILE189

site_id	CC1
Number of Residues	18
Details	BINDING SITE FOR RESIDUE HEC C 612

Chain	Residue
C	HIS124
C	THR128
C	ILE236
C	LEU240
C	GLN263
C	ILE266
C	ALA267
C	GLY270
C	MET273
C	VAL274
C	ASP304
C	CYS305
C	CYS308
C	HIS309
C	LYS314
C	PRO315
C	HOH657
C	HOH676

site_id	CC2
Number of Residues	11
Details	BINDING SITE FOR RESIDUE NS1 M 613

Chain	Residue
M	GLY117
M	THR121
M	VAL155
M	GLY159
M	CYS160
M	VAL173
M	PRO174
M	GLY176
M	ILE177
M	HIS180
M	BCB601

site_id	CC3
Number of Residues	12
Details	BINDING SITE FOR RESIDUE UQ1 L 614

Chain	Residue
L	LEU189
L	HIS190
L	LEU193
L	GLU212
L	ASN213
L	PHE216
L	TYR222
L	SER223
L	ILE224
L	GLY225
L	ALA226
L	ILE229

site_id	CC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE LDA M 615

Chain	Residue
H	ARG33
H	PRO54
H	ASP56
M	GLY205
M	PHE256

site_id	CC5
Number of Residues	2
Details	BINDING SITE FOR RESIDUE LDA H 616

Chain	Residue
L	LEU151
M	TYR195

Functional Information from PROSITE/UniProt

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

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

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	260
Details	Transmembrane: {"description":"Helical"}

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