Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3D38

Crystal structure of new trigonal form of photosynthetic reaction center from Blastochloris viridis. Crystals grown in microfluidics by detergent capture.

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 FE2 M 500

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

site_id	AC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 M 801

Chain	Residue
L	ASN199
M	HIS143
M	ARG265

site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 M 802

Chain	Residue
M	TYR50
M	GLY52
M	ALA53
M	SER54
M	SER133
M	TRP23

site_id	AC4
Number of Residues	2
Details	BINDING SITE FOR RESIDUE SO4 H 803

Chain	Residue
H	THR250
H	ARG253

site_id	AC5
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 M 804

Chain	Residue
H	LEU246
M	ALA1
M	ARG226

site_id	AC6
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 M 805

Chain	Residue
M	SER35
M	TYR36
M	TRP37

site_id	AC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 H 806

Chain	Residue
H	ARG37
H	TYR41
H	GLU61
M	ARG251

site_id	AC8
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 H 807

Chain	Residue
H	TYR117
H	GLU119
H	ARG233
H	LYS237

site_id	AC9
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 C 808

Chain	Residue
C	ALA319
C	SER320
C	ARG321

site_id	BC1
Number of Residues	2
Details	BINDING SITE FOR RESIDUE SO4 C 809

Chain	Residue
C	GLU112
C	ARG115

site_id	BC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 C 810

Chain	Residue
C	ASN196
C	LYS198
C	ARG199

site_id	BC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 C 811

Chain	Residue
C	HIS162
C	ARG165
L	ASP70
L	LYS72
L	TYR73
L	GLU82

site_id	BC4
Number of Residues	2
Details	BINDING SITE FOR RESIDUE SO4 H 812

Chain	Residue
H	HIS72
H	ASP129

site_id	BC5
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 C 813

Chain	Residue
C	THR161
C	HIS162
L	LYS72

site_id	BC6
Number of Residues	2
Details	BINDING SITE FOR RESIDUE SO4 C 814

Chain	Residue
C	LYS258
C	ARG293

site_id	BC7
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 C 815

Chain	Residue
C	PRO160
C	ARG165
M	PRO306

site_id	BC8
Number of Residues	19
Details	BINDING SITE FOR RESIDUE HEC C 401

Chain	Residue
C	TYR56
C	LYS57
C	ASN58
C	LYS60
C	LEU62
C	PHE70
C	LEU71
C	MET74
C	THR75
C	ILE77
C	THR78
C	CYS87
C	CYS90
C	HIS91
C	LEU96
C	ALA97
C	TYR104
C	ALA107
C	ARG108

site_id	BC9
Number of Residues	15
Details	BINDING SITE FOR RESIDUE HEC C 402

Chain	Residue
C	TYR89
C	TYR102
C	MET110
C	LEU111
C	MET113
C	THR114
C	THR131
C	CYS132
C	CYS135
C	HIS136
C	PRO140
C	LEU141
C	PRO142
C	ARG293
C	PRO301

site_id	CC1
Number of Residues	18
Details	BINDING SITE FOR RESIDUE HEC C 403

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

site_id	CC2
Number of Residues	16
Details	BINDING SITE FOR RESIDUE HEC C 404

Chain	Residue
C	HIS124
C	THR128
C	ILE236
C	LEU240
C	PHE246
C	GLN263
C	ILE266
C	GLY270
C	ILE271
C	MET273
C	CYS305
C	CYS308
C	HIS309
C	THR313
C	LYS314
C	PRO315

site_id	CC3
Number of Residues	18
Details	BINDING SITE FOR RESIDUE BCB L 400

Chain	Residue
L	PHE97
L	PRO124
L	MET127
L	PHE128
L	ASN158
L	PHE160
L	GLY161
L	TYR162
L	TRP167
L	HIS168
L	HIS173
L	SER176
L	ILE240
L	PHE241
L	GLY244
L	THR248
M	TYR195
M	TYR208

site_id	CC4
Number of Residues	10
Details	BINDING SITE FOR RESIDUE BCB L 401

Chain	Residue
L	PHE128
L	PHE146
L	ILE150
L	HIS153
L	LEU154
M	GLY201
M	ILE204
M	GLY205
M	TYR208
M	GLY209

site_id	CC5
Number of Residues	17
Details	BINDING SITE FOR RESIDUE BPB L 402

Chain	Residue
L	PHE41
L	ILE42
L	PHE97
L	TRP100
L	GLU104
L	PHE121
L	PRO124
L	TYR148
L	GLY149
L	ILE150
L	HIS153
L	ALA237
L	PHE241
M	TYR208
M	GLY211
M	LEU212
M	TRP250

site_id	CC6
Number of Residues	11
Details	BINDING SITE FOR RESIDUE MQ9 M 501

Chain	Residue
L	TYR29
L	ILE39
L	PHE43
L	TRP100
M	HIS217
M	ALA246
M	TRP250
M	ILE254
M	ASN257
M	ALA258
M	TRP266

site_id	CC7
Number of Residues	10
Details	BINDING SITE FOR RESIDUE UQ1 L 502

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

site_id	CC8
Number of Residues	4
Details	BINDING SITE FOR RESIDUE UQ1 L 503

Chain	Residue
L	TRP266
M	PHE85
M	PHE88
M	PHE89

site_id	CC9
Number of Residues	10
Details	BINDING SITE FOR RESIDUE BCB M 400

Chain	Residue
L	HIS168
L	MET174
L	SER178
L	PHE181
L	MET185
M	ILE177
M	TRP178
M	HIS180
M	ILE181
M	LEU184

site_id	DC1
Number of Residues	18
Details	BINDING SITE FOR RESIDUE BCB M 401

Chain	Residue
L	TYR162
L	PHE181
M	GLY62
M	LEU124
M	PHE154
M	LEU184
M	THR185
M	PHE187
M	SER188
M	PHE194
M	TYR195
M	HIS200
M	SER203
M	ILE204
M	TYR208
M	MET275
M	ALA278
M	ILE282

site_id	DC2
Number of Residues	13
Details	BINDING SITE FOR RESIDUE BPB M 402

Chain	Residue
L	PHE181
L	ALA184
L	MET185
L	LEU189
M	ALA58
M	PHE59
M	SER123
M	LEU124
M	TRP127
M	ILE144
M	ASN147
M	PHE148
M	SER271

site_id	DC3
Number of Residues	10
Details	BINDING SITE FOR RESIDUE NS5 M 600

Chain	Residue
M	LEU70
M	LEU114
M	GLY117
M	THR121
M	GLY159
M	CYS160
M	PHE175
M	GLY176
M	ILE177
M	HIS180

site_id	DC4
Number of Residues	2
Details	BINDING SITE FOR RESIDUE LDA H 701

Chain	Residue
H	ARG33
H	ASP56

site_id	DC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE LDA L 702

Chain	Residue
H	TRP17
L	ASP60
M	TYR195
M	PRO198
M	TRP295
M	HIS299

site_id	DC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE LDA H 703

Chain	Residue
H	LEU30
H	ARG34
H	TYR60
H	LEU62
H	TYR64

site_id	DC7
Number of Residues	2
Details	BINDING SITE FOR RESIDUE LDA M 704

Chain	Residue
M	ALA53
M	LEU122

site_id	DC8
Number of Residues	4
Details	BINDING SITE FOR RESIDUE HTO H 705

Chain	Residue
H	PRO71
H	HIS72
H	ASP125
H	ALA126

site_id	DC9
Number of Residues	3
Details	BINDING SITE FOR RESIDUE HTO C 706

Chain	Residue
C	PRO205
C	GLN206
C	ARG221

site_id	EC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE HTO C 707

Chain	Residue
C	GLU21
C	GLY241
C	THR313

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	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