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4CAS

Serial femtosecond crystallography structure of a photosynthetic reaction center

Functional Information from GO Data
ChainGOidnamespacecontents
A0005506molecular_functioniron ion binding
A0009055molecular_functionelectron transfer activity
A0019684biological_processphotosynthesis, light reaction
A0020037molecular_functionheme binding
A0030077cellular_componentplasma membrane light-harvesting complex
B0009772biological_processphotosynthetic electron transport in photosystem II
B0015979biological_processphotosynthesis
B0016168molecular_functionchlorophyll binding
B0019684biological_processphotosynthesis, light reaction
B0030077cellular_componentplasma membrane light-harvesting complex
B0042314molecular_functionbacteriochlorophyll binding
B0042717cellular_componentplasma membrane-derived chromatophore membrane
B0046872molecular_functionmetal ion binding
C0009772biological_processphotosynthetic electron transport in photosystem II
C0015979biological_processphotosynthesis
C0016168molecular_functionchlorophyll binding
C0019684biological_processphotosynthesis, light reaction
C0030077cellular_componentplasma membrane light-harvesting complex
C0042314molecular_functionbacteriochlorophyll binding
C0042717cellular_componentplasma membrane-derived chromatophore membrane
C0046872molecular_functionmetal ion binding
D0015979biological_processphotosynthesis
D0016168molecular_functionchlorophyll binding
D0019684biological_processphotosynthesis, light reaction
D0030077cellular_componentplasma membrane light-harvesting complex
D0042314molecular_functionbacteriochlorophyll binding
D0042717cellular_componentplasma membrane-derived chromatophore membrane
Functional Information from PDB Data
site_idAC1
Number of Residues17
Detailsbinding site for residue HEC A 401
ChainResidue
ATYR56
ATHR78
ASER82
ACYS87
ACYS90
AHIS91
ATYR104
AALA107
AARG108
ALYS57
AASN58
AVAL59
ALYS60
AVAL61
ALEU62
APHE70
AMET74

site_idAC2
Number of Residues17
Detailsbinding site for residue HEC A 402
ChainResidue
AVAL81
ATYR89
ATYR102
AVAL106
AMET110
AMET113
ATHR114
ACYS132
ACYS135
AHIS136
APRO140
ALEU141
APRO142
ALEU289
AARG293
APRO301
AHEC404

site_idAC3
Number of Residues18
Detailsbinding site for residue HEC A 403
ChainResidue
AVAL201
AARG202
AVAL203
AVAL204
AMET233
ASER237
AASN243
ACYS244
ACYS247
AHIS248
APHE253
AGLU254
AARG264
AALA267
ATRP268
AARG272
BTYR162
CILE189

site_idAC4
Number of Residues16
Detailsbinding site for residue HEC A 404
ChainResidue
AHIS124
ATHR128
AGLY129
ALEU240
AGLN263
AALA267
AILE271
AMET273
AASP304
ACYS305
ACYS308
AHIS309
ATHR313
ALYS314
APRO315
AHEC402

site_idAC5
Number of Residues3
Detailsbinding site for residue DGA A 405
ChainResidue
ACYS1
BTRP262
BTRP265

site_idAC6
Number of Residues11
Detailsbinding site for residue BCL B 301
ChainResidue
BMET174
BVAL177
BPHE181
BMET185
BBCL302
CMET120
CVAL155
CHIS180
CBCL402
CBPB403
CNS5405

site_idAC7
Number of Residues20
Detailsbinding site for residue BCL B 302
ChainResidue
BBPB304
CTYR195
CBCL402
BPHE97
BPRO124
BMET127
BPHE128
BLEU131
BVAL157
BASN158
BPHE160
BTRP167
BHIS168
BHIS173
BSER176
BPHE241
BGLY244
BTHR248
BBCL301
BBCL303

site_idAC8
Number of Residues16
Detailsbinding site for residue BCL B 303
ChainResidue
BILE49
BPHE128
BPHE146
BILE150
BHIS153
BLEU154
BVAL157
BBCL302
BBPB304
CTYR195
CGLY201
CILE204
CGLY205
CTYR208
CBCL402
COTP406

site_idAC9
Number of Residues18
Detailsbinding site for residue BPB B 304
ChainResidue
BILE42
BILE49
BALA93
BTRP100
BGLU104
BVAL117
BPHE121
BPRO124
BTYR148
BGLY149
BILE150
BHIS153
BALA237
BBCL302
BBCL303
CTYR208
CLEU212
CMQ7404

site_idAD1
Number of Residues3
Detailsbinding site for residue MPG B 305
ChainResidue
BLEU119
BSER238
CALA1

site_idAD2
Number of Residues5
Detailsbinding site for residue MPG B 306
ChainResidue
BPHE179
BLEU189
BHIS190
BPHE216
BSER223

site_idAD3
Number of Residues5
Detailsbinding site for residue FE2 C 401
ChainResidue
BHIS190
BHIS230
CHIS217
CGLU232
CHIS264

site_idAD4
Number of Residues19
Detailsbinding site for residue BCL C 402
ChainResidue
BHIS168
BBCL301
BBCL302
BBCL303
CILE69
CMET120
CPHE148
CPHE154
CTHR185
CPHE194
CTYR195
CHIS200
CSER203
CILE204
CTYR208
CMET275
CALA278
CILE282
CBPB403

site_idAD5
Number of Residues14
Detailsbinding site for residue BPB C 403
ChainResidue
BPHE181
BMET185
BLEU189
BBCL301
CSER63
CSER123
CTRP127
CILE144
CASN147
CPHE148
CSER271
CMET275
CBCL402
CNS5405

site_idAD6
Number of Residues12
Detailsbinding site for residue MQ7 C 404
ChainResidue
BTYR29
BILE39
BARG103
BBPB304
CHIS217
CTHR220
CALA246
CALA247
CTRP250
CASN257
CALA258
CTRP266

site_idAD7
Number of Residues8
Detailsbinding site for residue NS5 C 405
ChainResidue
BBCL301
CGLY117
CTHR121
CVAL155
CGLY159
CCYS160
CGLY176
CBPB403

site_idAD8
Number of Residues7
Detailsbinding site for residue OTP C 406
ChainResidue
BPHE62
BLEU151
BBCL303
CPRO198
CPHE206
CCYS296
DTRP25

site_idAD9
Number of Residues6
Detailsbinding site for residue PO4 C 408
ChainResidue
CTRP23
CTYR50
CGLY52
CALA53
CSER54
CSER133

site_idAE1
Number of Residues1
Detailsbinding site for residue PO4 C 409
ChainResidue
CARG265

Functional Information from PROSITE/UniProt
site_idPS00244
Number of Residues27
DetailsREACTION_CENTER Photosynthetic reaction center proteins signature. NfyycPwHgfSigfaygcgllfAaHGA
ChainResidueDetails
CASN193-ALA219
BASN166-GLY192

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsBinding site: {"description":"axial binding residue","evidences":[{"source":"PubMed","id":"22054235","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3T6E","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues8
DetailsBinding site: {"description":"covalent","evidences":[{"source":"PubMed","id":"22054235","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3T6E","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsSite: {"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"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsLipidation: {"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"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues147
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"2676514","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues260
DetailsTransmembrane: {"description":"Helical"}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues185
DetailsTopological domain: {"description":"Periplasmic","evidences":[{"source":"PubMed","id":"2676514","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues4
DetailsBinding site: {"description":"axial binding residue"}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues7
DetailsBinding site: {}
ChainResidueDetails

246704

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