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2BNS

Lipidic cubic phase grown reaction centre from Rhodobacter sphaeroides, excited state

Functional Information from GO Data
ChainGOidnamespacecontents
A0009772biological_processphotosynthetic electron transport in photosystem II
A0015979biological_processphotosynthesis
A0016020cellular_componentmembrane
A0016168molecular_functionchlorophyll binding
A0019684biological_processphotosynthesis, light reaction
A0030077cellular_componentplasma membrane light-harvesting complex
A0042314molecular_functionbacteriochlorophyll binding
A0042717cellular_componentplasma membrane-derived chromatophore membrane
A0045156molecular_functionelectron transporter, transferring electrons within the cyclic electron transport pathway of photosynthesis activity
A0046872molecular_functionmetal ion binding
B0009772biological_processphotosynthetic electron transport in photosystem II
B0015979biological_processphotosynthesis
B0016020cellular_componentmembrane
B0016168molecular_functionchlorophyll binding
B0019684biological_processphotosynthesis, light reaction
B0030077cellular_componentplasma membrane light-harvesting complex
B0042314molecular_functionbacteriochlorophyll binding
B0042717cellular_componentplasma membrane-derived chromatophore membrane
B0045156molecular_functionelectron transporter, transferring electrons within the cyclic electron transport pathway of photosynthesis activity
B0046872molecular_functionmetal ion binding
C0015979biological_processphotosynthesis
C0016020cellular_componentmembrane
C0016168molecular_functionchlorophyll binding
C0019684biological_processphotosynthesis, light reaction
C0030077cellular_componentplasma membrane light-harvesting complex
C0042314molecular_functionbacteriochlorophyll binding
C0042717cellular_componentplasma membrane-derived chromatophore membrane
C0045156molecular_functionelectron transporter, transferring electrons within the cyclic electron transport pathway of photosynthesis activity
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FE2 B 1305
ChainResidue
AHIS190
AHIS230
BHIS219
BGLU234
BHIS266

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PO4 B 1308
ChainResidue
AASN199
ALYS202
BHIS145
BARG267

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PO4 B 1309
ChainResidue
ALYS202
BGLY143
BLYS144
BTRP148
BHOH2027

site_idAC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL B 1307
ChainResidue
BARG132
BARG136

site_idAC5
Number of Residues18
DetailsBINDING SITE FOR RESIDUE BCL A 1282
ChainResidue
APHE97
AALA127
ATYR128
ALEU131
AVAL157
ATHR160
ATYR162
AASN166
AHIS168
AHIS173
AILE177
APHE180
ASER244
AMET248
ABCL1283
ABPH1284
BBCL1302
BBCL1303

site_idAC6
Number of Residues16
DetailsBINDING SITE FOR RESIDUE BCL A 1283
ChainResidue
ATYR128
ALEU131
APHE146
AILE150
AHIS153
ALEU154
ABCL1282
ABPH1284
AHOH2036
BPHE197
BGLY203
BILE206
BALA207
BTYR210
BGLY211
BBCL1303

site_idAC7
Number of Residues15
DetailsBINDING SITE FOR RESIDUE BPH A 1284
ChainResidue
APHE97
ATRP100
AGLU104
AILE117
APHE121
AALA124
AHIS153
AVAL241
ABCL1282
ABCL1283
BTYR210
BALA213
BLEU214
BTRP252
BMET256

site_idAC8
Number of Residues10
DetailsBINDING SITE FOR RESIDUE MST A 1285
ChainResidue
ALEU189
ALEU193
AGLU212
AASP213
APHE216
ATYR222
ASER223
AILE224
AGLY225
AILE229

site_idAC9
Number of Residues13
DetailsBINDING SITE FOR RESIDUE BCL B 1302
ChainResidue
AMET174
AILE177
ASER178
ATHR182
ABCL1282
AHOH2021
BTRP157
BILE179
BHIS182
BLEU183
BTHR186
BBCL1303
BBPH1304

site_idBC1
Number of Residues22
DetailsBINDING SITE FOR RESIDUE BCL B 1303
ChainResidue
BLEU196
BPHE197
BHIS202
BSER205
BILE206
BTYR210
BVAL276
BGLY280
BILE284
BBCL1302
BBPH1304
AVAL157
ATYR162
APHE181
ABCL1282
ABCL1283
BALA153
BLEU156
BLEU160
BTHR186
BASN187
BPHE189

site_idBC2
Number of Residues14
DetailsBINDING SITE FOR RESIDUE BPH B 1304
ChainResidue
APHE181
AALA184
ALEU185
ALEU189
ALEU219
BGLY63
BTRP129
BTHR146
BALA149
BPHE150
BALA273
BTHR277
BBCL1302
BBCL1303

site_idBC3
Number of Residues13
DetailsBINDING SITE FOR RESIDUE U10 B 1306
ChainResidue
BMET218
BHIS219
BTHR222
BALA248
BALA249
BTRP252
BMET256
BPHE258
BASN259
BALA260
BILE265
BTRP268
BMET272

Functional Information from PROSITE/UniProt
site_idPS00244
Number of Residues27
DetailsREACTION_CENTER Photosynthetic reaction center proteins signature. NfhynPaHmiAisffftnalalAlHGA
ChainResidueDetails
AASN166-ALA192
BASN195-ALA221

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues10
DetailsTOPO_DOM: Periplasmic
ChainResidueDetails
CMET1-ASP11
BMET142-LEU167
BPHE197-ALA225
BASN259-LEU285
BLYS110-ALA139

site_idSWS_FT_FI2
Number of Residues19
DetailsTRANSMEM: Helical
ChainResidueDetails
AGLY225-ILE250
CLEU12-LEU31
BHIS202
AHIS116-MET138
APRO171-ALA198

site_idSWS_FT_FI3
Number of Residues228
DetailsTOPO_DOM: Cytoplasmic
ChainResidueDetails
CGLN32-ALA260
BGLU234
BHIS266
BTRP252

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: axial binding residue
ChainResidueDetails
AHIS173
AHIS153

site_idSWS_FT_FI5
Number of Residues3
DetailsBINDING:
ChainResidueDetails
AHIS190
AHIS230
APHE216

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PDB entries from 2024-04-17

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