6WJ6
Cryo-EM structure of apo-Photosystem II from Synechocystis sp. PCC 6803
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005506 | molecular_function | iron ion binding |
| A | 0009055 | molecular_function | electron transfer activity |
| A | 0009523 | cellular_component | photosystem II |
| A | 0009635 | biological_process | response to herbicide |
| A | 0009772 | biological_process | photosynthetic electron transport in photosystem II |
| A | 0010242 | molecular_function | oxygen evolving activity |
| A | 0015979 | biological_process | photosynthesis |
| A | 0016168 | molecular_function | chlorophyll binding |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016682 | molecular_function | oxidoreductase activity, acting on diphenols and related substances as donors, oxygen as acceptor |
| A | 0019684 | biological_process | photosynthesis, light reaction |
| A | 0030096 | cellular_component | plasma membrane-derived thylakoid photosystem II |
| A | 0031676 | cellular_component | plasma membrane-derived thylakoid membrane |
| A | 0042651 | cellular_component | thylakoid membrane |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0009521 | cellular_component | photosystem |
| B | 0009523 | cellular_component | photosystem II |
| B | 0009579 | cellular_component | thylakoid |
| B | 0009767 | biological_process | photosynthetic electron transport chain |
| B | 0009772 | biological_process | photosynthetic electron transport in photosystem II |
| B | 0015979 | biological_process | photosynthesis |
| B | 0016020 | cellular_component | membrane |
| B | 0016168 | molecular_function | chlorophyll binding |
| B | 0019684 | biological_process | photosynthesis, light reaction |
| B | 0030096 | cellular_component | plasma membrane-derived thylakoid photosystem II |
| B | 0031676 | cellular_component | plasma membrane-derived thylakoid membrane |
| B | 0042651 | cellular_component | thylakoid membrane |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0009521 | cellular_component | photosystem |
| C | 0009523 | cellular_component | photosystem II |
| C | 0009579 | cellular_component | thylakoid |
| C | 0009767 | biological_process | photosynthetic electron transport chain |
| C | 0009772 | biological_process | photosynthetic electron transport in photosystem II |
| C | 0015979 | biological_process | photosynthesis |
| C | 0016020 | cellular_component | membrane |
| C | 0016168 | molecular_function | chlorophyll binding |
| C | 0019684 | biological_process | photosynthesis, light reaction |
| C | 0030096 | cellular_component | plasma membrane-derived thylakoid photosystem II |
| C | 0031676 | cellular_component | plasma membrane-derived thylakoid membrane |
| C | 0042651 | cellular_component | thylakoid membrane |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0005506 | molecular_function | iron ion binding |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0009055 | molecular_function | electron transfer activity |
| D | 0009523 | cellular_component | photosystem II |
| D | 0009772 | biological_process | photosynthetic electron transport in photosystem II |
| D | 0010242 | molecular_function | oxygen evolving activity |
| D | 0015979 | biological_process | photosynthesis |
| D | 0016020 | cellular_component | membrane |
| D | 0016168 | molecular_function | chlorophyll binding |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0019684 | biological_process | photosynthesis, light reaction |
| D | 0030096 | cellular_component | plasma membrane-derived thylakoid photosystem II |
| D | 0031676 | cellular_component | plasma membrane-derived thylakoid membrane |
| D | 0042651 | cellular_component | thylakoid membrane |
| D | 0046872 | molecular_function | metal ion binding |
| E | 0005506 | molecular_function | iron ion binding |
| E | 0005737 | cellular_component | cytoplasm |
| E | 0009055 | molecular_function | electron transfer activity |
| E | 0009523 | cellular_component | photosystem II |
| E | 0009539 | cellular_component | photosystem II reaction center |
| E | 0009579 | cellular_component | thylakoid |
| E | 0009767 | biological_process | photosynthetic electron transport chain |
| E | 0015979 | biological_process | photosynthesis |
| E | 0016020 | cellular_component | membrane |
| E | 0019684 | biological_process | photosynthesis, light reaction |
| E | 0020037 | molecular_function | heme binding |
| E | 0030096 | cellular_component | plasma membrane-derived thylakoid photosystem II |
| E | 0031676 | cellular_component | plasma membrane-derived thylakoid membrane |
| E | 0042651 | cellular_component | thylakoid membrane |
| E | 0046872 | molecular_function | metal ion binding |
| F | 0005506 | molecular_function | iron ion binding |
| F | 0005737 | cellular_component | cytoplasm |
| F | 0009055 | molecular_function | electron transfer activity |
| F | 0009523 | cellular_component | photosystem II |
| F | 0009539 | cellular_component | photosystem II reaction center |
| F | 0009579 | cellular_component | thylakoid |
| F | 0009767 | biological_process | photosynthetic electron transport chain |
| F | 0015979 | biological_process | photosynthesis |
| F | 0016020 | cellular_component | membrane |
| F | 0019684 | biological_process | photosynthesis, light reaction |
| F | 0020037 | molecular_function | heme binding |
| F | 0030096 | cellular_component | plasma membrane-derived thylakoid photosystem II |
| F | 0031676 | cellular_component | plasma membrane-derived thylakoid membrane |
| F | 0042651 | cellular_component | thylakoid membrane |
| F | 0042802 | molecular_function | identical protein binding |
| F | 0046872 | molecular_function | metal ion binding |
| H | 0009523 | cellular_component | photosystem II |
| H | 0015979 | biological_process | photosynthesis |
| H | 0016020 | cellular_component | membrane |
| H | 0030096 | cellular_component | plasma membrane-derived thylakoid photosystem II |
| H | 0031676 | cellular_component | plasma membrane-derived thylakoid membrane |
| H | 0042301 | molecular_function | phosphate ion binding |
| H | 0042651 | cellular_component | thylakoid membrane |
| H | 0050821 | biological_process | protein stabilization |
| I | 0005737 | cellular_component | cytoplasm |
| I | 0009523 | cellular_component | photosystem II |
| I | 0009539 | cellular_component | photosystem II reaction center |
| I | 0015979 | biological_process | photosynthesis |
| I | 0016020 | cellular_component | membrane |
| I | 0030096 | cellular_component | plasma membrane-derived thylakoid photosystem II |
| I | 0031676 | cellular_component | plasma membrane-derived thylakoid membrane |
| I | 0042651 | cellular_component | thylakoid membrane |
| K | 0005737 | cellular_component | cytoplasm |
| K | 0009523 | cellular_component | photosystem II |
| K | 0009539 | cellular_component | photosystem II reaction center |
| K | 0015979 | biological_process | photosynthesis |
| K | 0030096 | cellular_component | plasma membrane-derived thylakoid photosystem II |
| K | 0031676 | cellular_component | plasma membrane-derived thylakoid membrane |
| K | 0042651 | cellular_component | thylakoid membrane |
| L | 0005737 | cellular_component | cytoplasm |
| L | 0009523 | cellular_component | photosystem II |
| L | 0009539 | cellular_component | photosystem II reaction center |
| L | 0009579 | cellular_component | thylakoid |
| L | 0015979 | biological_process | photosynthesis |
| L | 0016020 | cellular_component | membrane |
| L | 0030096 | cellular_component | plasma membrane-derived thylakoid photosystem II |
| L | 0031676 | cellular_component | plasma membrane-derived thylakoid membrane |
| L | 0042651 | cellular_component | thylakoid membrane |
| M | 0005737 | cellular_component | cytoplasm |
| M | 0009523 | cellular_component | photosystem II |
| M | 0015979 | biological_process | photosynthesis |
| M | 0016020 | cellular_component | membrane |
| M | 0019684 | biological_process | photosynthesis, light reaction |
| M | 0030096 | cellular_component | plasma membrane-derived thylakoid photosystem II |
| M | 0031676 | cellular_component | plasma membrane-derived thylakoid membrane |
| M | 0042651 | cellular_component | thylakoid membrane |
| T | 0005737 | cellular_component | cytoplasm |
| T | 0009523 | cellular_component | photosystem II |
| T | 0009539 | cellular_component | photosystem II reaction center |
| T | 0015979 | biological_process | photosynthesis |
| T | 0016020 | cellular_component | membrane |
| T | 0030096 | cellular_component | plasma membrane-derived thylakoid photosystem II |
| T | 0031676 | cellular_component | plasma membrane-derived thylakoid membrane |
| T | 0042651 | cellular_component | thylakoid membrane |
| X | 0009523 | cellular_component | photosystem II |
| X | 0015979 | biological_process | photosynthesis |
| X | 0016020 | cellular_component | membrane |
| X | 0030096 | cellular_component | plasma membrane-derived thylakoid photosystem II |
| X | 0031676 | cellular_component | plasma membrane-derived thylakoid membrane |
| X | 0042651 | cellular_component | thylakoid membrane |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | binding site for residue FE2 A 401 |
| Chain | Residue |
| A | HIS215 |
| A | HIS272 |
| D | HIS214 |
| D | HIS268 |
| D | BCT404 |
| site_id | AC2 |
| Number of Residues | 21 |
| Details | binding site for residue CLA A 402 |
| Chain | Residue |
| A | MET183 |
| A | PHE186 |
| A | GLN187 |
| A | ILE192 |
| A | HIS198 |
| A | GLY201 |
| A | VAL205 |
| A | PHE206 |
| A | ILE283 |
| A | THR286 |
| A | VAL290 |
| A | CLA403 |
| A | PHO404 |
| D | ILE182 |
| D | CLA402 |
| D | CLA405 |
| D | LHG410 |
| A | TYR147 |
| A | PRO150 |
| A | ALA153 |
| A | VAL157 |
| site_id | AC3 |
| Number of Residues | 13 |
| Details | binding site for residue CLA A 403 |
| Chain | Residue |
| A | MET199 |
| A | VAL202 |
| A | ALA203 |
| A | GLY207 |
| A | TRP278 |
| A | CLA402 |
| D | VAL175 |
| D | ILE178 |
| D | PHE179 |
| D | ILE182 |
| D | PHO403 |
| D | CLA405 |
| D | HOH540 |
| site_id | AC4 |
| Number of Residues | 19 |
| Details | binding site for residue PHO A 404 |
| Chain | Residue |
| A | LEU41 |
| A | ALA44 |
| A | THR45 |
| A | PHE48 |
| A | TYR126 |
| A | GLN130 |
| A | TYR147 |
| A | PRO150 |
| A | GLY175 |
| A | PRO279 |
| A | CLA402 |
| A | SQD409 |
| D | ALA208 |
| D | LEU209 |
| D | ILE213 |
| D | TRP253 |
| D | CLA402 |
| D | PL9408 |
| D | LHG410 |
| site_id | AC5 |
| Number of Residues | 19 |
| Details | binding site for residue CLA A 405 |
| Chain | Residue |
| A | LEU36 |
| A | THR40 |
| A | THR43 |
| A | PHE93 |
| A | TYR94 |
| A | PRO95 |
| A | ILE96 |
| A | TRP97 |
| A | LEU114 |
| A | HIS118 |
| A | ILE121 |
| A | BCR406 |
| C | LMG501 |
| C | CLA506 |
| I | VAL8 |
| I | TYR9 |
| I | VAL11 |
| I | VAL12 |
| I | PHE15 |
| site_id | AC6 |
| Number of Residues | 10 |
| Details | binding site for residue BCR A 406 |
| Chain | Residue |
| A | LEU42 |
| A | THR43 |
| A | ILE50 |
| A | ALA51 |
| A | ALA54 |
| A | ILE96 |
| A | TRP105 |
| A | LEU106 |
| A | PRO111 |
| A | CLA405 |
| site_id | AC7 |
| Number of Residues | 14 |
| Details | binding site for residue SQD A 407 |
| Chain | Residue |
| D | ARG233 |
| D | LHG411 |
| A | LEU200 |
| A | PHE265 |
| A | SER270 |
| A | PHE273 |
| A | PHE274 |
| A | TRP278 |
| A | ILE281 |
| A | GLY282 |
| C | ALA21 |
| C | TRP23 |
| D | ASN230 |
| D | PHE232 |
| site_id | AC8 |
| Number of Residues | 8 |
| Details | binding site for residue PL9 A 408 |
| Chain | Residue |
| A | PHE211 |
| A | HIS215 |
| A | LEU218 |
| A | HIS252 |
| A | SER264 |
| A | PHE265 |
| A | LEU271 |
| A | LEU275 |
| site_id | AC9 |
| Number of Residues | 9 |
| Details | binding site for residue SQD A 409 |
| Chain | Residue |
| A | TRP20 |
| A | ASN26 |
| A | ARG27 |
| A | ILE28 |
| A | LEU42 |
| A | THR45 |
| A | PHO404 |
| D | CLA402 |
| T | SQD103 |
| site_id | AD1 |
| Number of Residues | 7 |
| Details | binding site for residue CLA B 601 |
| Chain | Residue |
| B | GLY186 |
| B | PRO187 |
| B | PHE190 |
| B | CLA602 |
| B | HOH704 |
| H | PHE41 |
| X | BCR102 |
| site_id | AD2 |
| Number of Residues | 17 |
| Details | binding site for residue CLA B 602 |
| Chain | Residue |
| B | GLY189 |
| B | PHE190 |
| B | GLY197 |
| B | ALA200 |
| B | HIS201 |
| B | ALA204 |
| B | VAL208 |
| B | PHE247 |
| B | PHE250 |
| B | VAL251 |
| B | CLA601 |
| B | CLA603 |
| H | PHE41 |
| H | ILE45 |
| H | LEU46 |
| H | TYR49 |
| H | DGD101 |
| site_id | AD3 |
| Number of Residues | 21 |
| Details | binding site for residue CLA B 603 |
| Chain | Residue |
| B | ARG68 |
| B | LEU69 |
| B | SER146 |
| B | LEU149 |
| B | CYS150 |
| B | PHE153 |
| B | MET166 |
| B | VAL198 |
| B | HIS201 |
| B | HIS202 |
| B | PHE247 |
| B | ALA248 |
| B | VAL252 |
| B | THR262 |
| B | CLA602 |
| B | CLA604 |
| B | CLA605 |
| B | CLA606 |
| B | CLA610 |
| H | PHE38 |
| H | LEU39 |
| site_id | AD4 |
| Number of Residues | 18 |
| Details | binding site for residue CLA B 604 |
| Chain | Residue |
| B | TRP33 |
| B | PHE61 |
| B | PHE65 |
| B | ARG68 |
| B | LEU149 |
| B | ALA248 |
| B | ALA249 |
| B | VAL252 |
| B | PHE451 |
| B | HIS455 |
| B | PHE458 |
| B | PHE462 |
| B | CLA603 |
| B | CLA605 |
| B | CLA607 |
| B | CLA612 |
| B | CLA613 |
| B | CLA615 |
| site_id | AD5 |
| Number of Residues | 22 |
| Details | binding site for residue CLA B 605 |
| Chain | Residue |
| B | THR27 |
| B | VAL30 |
| B | ALA31 |
| B | TRP33 |
| B | ALA34 |
| B | VAL62 |
| B | PHE65 |
| B | MET66 |
| B | ARG68 |
| B | VAL96 |
| B | HIS100 |
| B | LEU103 |
| B | LEU143 |
| B | ALA205 |
| B | CLA603 |
| B | CLA604 |
| B | CLA606 |
| B | CLA610 |
| B | CLA612 |
| B | CLA615 |
| B | BCR619 |
| B | HOH722 |
| site_id | AD6 |
| Number of Residues | 15 |
| Details | binding site for residue CLA B 606 |
| Chain | Residue |
| B | LEU69 |
| B | PHE90 |
| B | TRP91 |
| B | VAL96 |
| B | ALA99 |
| B | HIS100 |
| B | GLY152 |
| B | PHE153 |
| B | HIS157 |
| B | TRP162 |
| B | PRO164 |
| B | CLA603 |
| B | CLA605 |
| B | BCR619 |
| B | LMT622 |
| site_id | AD7 |
| Number of Residues | 21 |
| Details | binding site for residue CLA B 607 |
| Chain | Residue |
| B | TRP33 |
| B | MET37 |
| B | TYR40 |
| B | ILE44 |
| B | GLN58 |
| B | GLY59 |
| B | PHE61 |
| B | THR327 |
| B | GLY328 |
| B | TRP450 |
| B | PHE451 |
| B | CLA604 |
| B | CLA613 |
| B | BCR617 |
| B | BCR618 |
| B | LMG621 |
| B | HOH760 |
| D | MET281 |
| D | PL9408 |
| L | PHE37 |
| M | PHE14 |
| site_id | AD8 |
| Number of Residues | 19 |
| Details | binding site for residue CLA B 608 |
| Chain | Residue |
| B | THR236 |
| B | SER239 |
| B | SER240 |
| B | ALA243 |
| B | PHE247 |
| B | PHE463 |
| B | HIS466 |
| B | THR473 |
| B | LEU474 |
| B | CLA609 |
| B | CLA610 |
| B | SQD620 |
| B | HOH707 |
| D | PHE120 |
| D | ILE123 |
| D | MET126 |
| D | LEU127 |
| D | CLA406 |
| H | LEU43 |
| site_id | AD9 |
| Number of Residues | 17 |
| Details | binding site for residue CLA B 609 |
| Chain | Residue |
| B | PHE139 |
| B | VAL208 |
| B | ALA212 |
| B | PHE215 |
| B | HIS216 |
| B | VAL219 |
| B | PRO222 |
| B | LEU225 |
| B | LEU229 |
| B | CLA608 |
| B | CLA610 |
| B | SQD620 |
| H | THR27 |
| H | MET31 |
| H | PHE34 |
| H | LEU42 |
| X | BCR102 |
| site_id | AE1 |
| Number of Residues | 18 |
| Details | binding site for residue CLA B 610 |
| Chain | Residue |
| B | LEU135 |
| B | MET138 |
| B | PHE139 |
| B | HIS142 |
| B | LEU143 |
| B | SER146 |
| B | LEU229 |
| B | MET231 |
| B | VAL237 |
| B | SER240 |
| B | SER241 |
| B | CLA603 |
| B | CLA605 |
| B | CLA608 |
| B | CLA609 |
| B | CLA612 |
| B | CLA615 |
| B | HOH726 |
| site_id | AE2 |
| Number of Residues | 19 |
| Details | binding site for residue CLA B 611 |
| Chain | Residue |
| B | TRP5 |
| B | TYR6 |
| B | ARG7 |
| B | VAL8 |
| B | HIS9 |
| B | THR10 |
| B | LEU238 |
| B | LEU461 |
| B | PHE462 |
| B | PHE464 |
| B | GLY465 |
| B | TRP468 |
| B | HIS469 |
| B | ARG472 |
| B | CLA612 |
| B | CLA613 |
| B | CLA614 |
| D | LHG409 |
| L | LHG101 |
| site_id | AE3 |
| Number of Residues | 18 |
| Details | binding site for residue CLA B 612 |
| Chain | Residue |
| B | HIS9 |
| B | VAL12 |
| B | LEU13 |
| B | LEU19 |
| B | VAL22 |
| B | HIS23 |
| B | HIS26 |
| B | THR27 |
| B | VAL237 |
| B | LEU238 |
| B | SER241 |
| B | CLA604 |
| B | CLA605 |
| B | CLA610 |
| B | CLA611 |
| B | CLA613 |
| B | CLA614 |
| B | CLA615 |
| site_id | AE4 |
| Number of Residues | 13 |
| Details | binding site for residue CLA B 613 |
| Chain | Residue |
| B | HIS9 |
| B | HIS26 |
| B | VAL30 |
| B | TRP33 |
| B | PHE462 |
| B | CLA604 |
| B | CLA607 |
| B | CLA611 |
| B | CLA612 |
| B | CLA614 |
| B | BCR617 |
| B | BCR618 |
| D | LHG409 |
| site_id | AE5 |
| Number of Residues | 15 |
| Details | binding site for residue CLA B 614 |
| Chain | Residue |
| B | VAL8 |
| B | HIS9 |
| B | VAL11 |
| B | VAL22 |
| B | MET25 |
| B | LEU29 |
| B | TRP115 |
| B | CLA611 |
| B | CLA612 |
| B | CLA613 |
| B | BCR617 |
| L | GLN10 |
| L | VAL12 |
| M | PHE21 |
| M | LEU25 |
| site_id | AE6 |
| Number of Residues | 15 |
| Details | binding site for residue CLA B 615 |
| Chain | Residue |
| B | HIS23 |
| B | LEU24 |
| B | MET138 |
| B | ILE141 |
| B | HIS142 |
| B | LEU145 |
| B | CLA604 |
| B | CLA605 |
| B | CLA610 |
| B | CLA612 |
| B | CLA616 |
| B | BCR619 |
| H | LEU7 |
| H | LEU14 |
| H | ASN15 |
| site_id | AE7 |
| Number of Residues | 11 |
| Details | binding site for residue CLA B 616 |
| Chain | Residue |
| B | ILE20 |
| B | LEU24 |
| B | ALA110 |
| B | TRP113 |
| B | HIS114 |
| B | LEU120 |
| B | CLA615 |
| B | BCR619 |
| H | THR5 |
| H | LEU7 |
| H | GLY8 |
| site_id | AE8 |
| Number of Residues | 11 |
| Details | binding site for residue BCR B 617 |
| Chain | Residue |
| B | MET25 |
| B | LEU29 |
| B | PHE108 |
| B | ALA111 |
| B | VAL112 |
| B | TRP115 |
| B | CLA607 |
| B | CLA613 |
| B | CLA614 |
| B | LMG621 |
| M | ILE9 |
| site_id | AE9 |
| Number of Residues | 7 |
| Details | binding site for residue BCR B 618 |
| Chain | Residue |
| B | LEU29 |
| B | GLY32 |
| B | ILE101 |
| B | GLY105 |
| B | CLA607 |
| B | CLA613 |
| B | LMG621 |
| site_id | AF1 |
| Number of Residues | 10 |
| Details | binding site for residue BCR B 619 |
| Chain | Residue |
| B | LEU107 |
| B | LEU109 |
| B | VAL112 |
| B | TRP113 |
| B | PHE117 |
| B | CLA605 |
| B | CLA606 |
| B | CLA615 |
| B | CLA616 |
| B | LMT622 |
| site_id | AF2 |
| Number of Residues | 7 |
| Details | binding site for residue SQD B 620 |
| Chain | Residue |
| B | ARG224 |
| B | LYS227 |
| B | ALA228 |
| B | ARG230 |
| B | CLA608 |
| B | CLA609 |
| H | TRP25 |
| site_id | AF3 |
| Number of Residues | 13 |
| Details | binding site for residue LMG B 621 |
| Chain | Residue |
| B | THR327 |
| B | GLY328 |
| B | ALA329 |
| B | SER332 |
| B | GLY454 |
| B | VAL457 |
| B | CLA607 |
| B | BCR617 |
| B | BCR618 |
| L | PHE37 |
| M | ASN4 |
| M | LEU6 |
| M | ALA10 |
| site_id | AF4 |
| Number of Residues | 7 |
| Details | binding site for residue LMT B 622 |
| Chain | Residue |
| B | PRO88 |
| B | TRP91 |
| B | LEU149 |
| B | TRP162 |
| B | CLA606 |
| B | BCR619 |
| B | LMT623 |
| site_id | AF5 |
| Number of Residues | 6 |
| Details | binding site for residue LMT B 623 |
| Chain | Residue |
| B | LEU148 |
| B | GLY152 |
| B | PHE156 |
| B | VAL161 |
| B | TRP162 |
| B | LMT622 |
| site_id | AF6 |
| Number of Residues | 17 |
| Details | binding site for residue LMG C 501 |
| Chain | Residue |
| A | PHE93 |
| A | TRP97 |
| A | GLU98 |
| A | ILE121 |
| A | PHE124 |
| A | CLA405 |
| C | LEU201 |
| C | LYS202 |
| C | PHE205 |
| C | GLU208 |
| C | TRP210 |
| C | LEU268 |
| C | CLA506 |
| C | CLA507 |
| C | DGD517 |
| I | LYS5 |
| I | TYR9 |
| site_id | AF7 |
| Number of Residues | 17 |
| Details | binding site for residue CLA C 502 |
| Chain | Residue |
| C | LEU82 |
| C | LEU155 |
| C | GLY158 |
| C | ALA159 |
| C | LEU162 |
| C | ILE220 |
| C | HIS224 |
| C | ILE227 |
| C | MET269 |
| C | PHE276 |
| C | ALA283 |
| C | TYR284 |
| C | CLA503 |
| C | CLA504 |
| C | CLA507 |
| C | CLA508 |
| C | BCR516 |
| site_id | AF8 |
| Number of Residues | 17 |
| Details | binding site for residue CLA C 503 |
| Chain | Residue |
| C | TRP50 |
| C | LEU75 |
| C | HIS78 |
| C | TRP84 |
| C | LYS165 |
| C | LEU266 |
| C | MET269 |
| C | ALA273 |
| C | TYR284 |
| C | HIS417 |
| C | LEU420 |
| C | PHE424 |
| C | CLA502 |
| C | CLA504 |
| C | CLA505 |
| C | CLA511 |
| C | CLA513 |
| site_id | AF9 |
| Number of Residues | 15 |
| Details | binding site for residue CLA C 504 |
| Chain | Residue |
| C | ILE47 |
| C | VAL48 |
| C | TRP50 |
| C | ALA51 |
| C | THR55 |
| C | LEU75 |
| C | TRP84 |
| C | VAL101 |
| C | HIS105 |
| C | CLA502 |
| C | CLA503 |
| C | CLA510 |
| C | CLA511 |
| C | CLA513 |
| C | SQD518 |
| site_id | AG1 |
| Number of Residues | 15 |
| Details | binding site for residue CLA C 505 |
| Chain | Residue |
| C | TRP50 |
| C | MET54 |
| C | PHE57 |
| C | GLY72 |
| C | LEU73 |
| C | ILE74 |
| C | TRP412 |
| C | SER416 |
| C | HIS417 |
| C | PHE423 |
| C | CLA503 |
| C | CLA511 |
| C | HOH624 |
| K | PRO25 |
| K | LEU29 |
| site_id | AG2 |
| Number of Residues | 16 |
| Details | binding site for residue CLA C 506 |
| Chain | Residue |
| A | PHE33 |
| A | PHE124 |
| A | TRP131 |
| A | CLA405 |
| C | LEU251 |
| C | SER260 |
| C | TYR261 |
| C | GLY264 |
| C | HIS428 |
| C | LEU429 |
| C | ALA432 |
| C | ARG436 |
| C | LMG501 |
| C | CLA508 |
| C | BCR516 |
| I | PHE23 |
| site_id | AG3 |
| Number of Residues | 15 |
| Details | binding site for residue CLA C 507 |
| Chain | Residue |
| C | ILE148 |
| C | LEU152 |
| C | ILE230 |
| C | GLY234 |
| C | HIS238 |
| C | THR241 |
| C | LYS242 |
| C | PRO243 |
| C | PHE244 |
| C | TRP246 |
| C | ALA247 |
| C | LMG501 |
| C | CLA502 |
| C | CLA508 |
| C | BCR516 |
| site_id | AG4 |
| Number of Residues | 19 |
| Details | binding site for residue CLA C 508 |
| Chain | Residue |
| C | MET144 |
| C | THR145 |
| C | ILE147 |
| C | ILE148 |
| C | HIS151 |
| C | LEU155 |
| C | CYS231 |
| C | LEU251 |
| C | TRP253 |
| C | TYR258 |
| C | TYR261 |
| C | SER262 |
| C | MET269 |
| C | CLA502 |
| C | CLA506 |
| C | CLA507 |
| C | CLA510 |
| C | BCR516 |
| C | HOH601 |
| site_id | AG5 |
| Number of Residues | 19 |
| Details | binding site for residue CLA C 509 |
| Chain | Residue |
| C | PHE20 |
| C | TRP23 |
| C | SER24 |
| C | GLY25 |
| C | ASN26 |
| C | ALA27 |
| C | LEU259 |
| C | LEU263 |
| C | PHE423 |
| C | PHE424 |
| C | GLY427 |
| C | TRP430 |
| C | HIS431 |
| C | ARG434 |
| C | CLA510 |
| C | CLA511 |
| C | CLA512 |
| D | LHG411 |
| K | PHE36 |
| site_id | AG6 |
| Number of Residues | 19 |
| Details | binding site for residue CLA C 510 |
| Chain | Residue |
| C | ASN26 |
| C | ILE30 |
| C | LEU36 |
| C | ALA39 |
| C | HIS40 |
| C | HIS43 |
| C | TRP138 |
| C | GLY255 |
| C | GLU256 |
| C | TYR258 |
| C | LEU259 |
| C | SER262 |
| C | LEU266 |
| C | CLA504 |
| C | CLA508 |
| C | CLA509 |
| C | CLA511 |
| C | CLA512 |
| C | CLA513 |
| site_id | AG7 |
| Number of Residues | 15 |
| Details | binding site for residue CLA C 511 |
| Chain | Residue |
| C | ASN26 |
| C | HIS43 |
| C | LEU46 |
| C | ILE47 |
| C | TRP50 |
| C | LEU266 |
| C | PHE424 |
| C | CLA503 |
| C | CLA504 |
| C | CLA505 |
| C | CLA509 |
| C | CLA510 |
| C | CLA512 |
| K | PRO28 |
| K | LEU32 |
| site_id | AG8 |
| Number of Residues | 14 |
| Details | binding site for residue CLA C 512 |
| Chain | Residue |
| C | TRP22 |
| C | GLY25 |
| C | ASN26 |
| C | ARG28 |
| C | LEU29 |
| C | LYS35 |
| C | ALA39 |
| C | LEU46 |
| C | ALA120 |
| C | CLA509 |
| C | CLA510 |
| C | CLA511 |
| C | BCR519 |
| K | GLN39 |
| site_id | AG9 |
| Number of Residues | 17 |
| Details | binding site for residue CLA C 513 |
| Chain | Residue |
| C | HIS40 |
| C | VAL41 |
| C | ALA44 |
| C | LEU112 |
| C | PHE133 |
| C | PHE134 |
| C | TYR136 |
| C | ILE147 |
| C | TYR150 |
| C | HIS151 |
| C | LEU154 |
| C | LEU161 |
| C | CLA503 |
| C | CLA504 |
| C | CLA510 |
| C | CLA514 |
| C | SQD518 |
| site_id | AH1 |
| Number of Residues | 12 |
| Details | binding site for residue CLA C 514 |
| Chain | Residue |
| C | LEU37 |
| C | VAL41 |
| C | VAL111 |
| C | LEU112 |
| C | GLY115 |
| C | TYR118 |
| C | HIS119 |
| C | TYR130 |
| C | PHE134 |
| C | CLA513 |
| C | BCR515 |
| C | SQD518 |
| site_id | AH2 |
| Number of Residues | 9 |
| Details | binding site for residue BCR C 515 |
| Chain | Residue |
| C | PHE99 |
| C | VAL103 |
| C | ILE107 |
| C | SER108 |
| C | VAL111 |
| C | PHE134 |
| C | CLA514 |
| C | SQD518 |
| K | TYR14 |
| site_id | AH3 |
| Number of Residues | 13 |
| Details | binding site for residue BCR C 516 |
| Chain | Residue |
| C | ILE196 |
| C | PHE197 |
| C | LEU200 |
| C | ASP219 |
| C | GLY223 |
| C | HIS224 |
| C | ILE227 |
| C | LEU251 |
| C | CLA502 |
| C | CLA506 |
| C | CLA507 |
| C | CLA508 |
| I | LEU24 |
| site_id | AH4 |
| Number of Residues | 21 |
| Details | binding site for residue DGD C 517 |
| Chain | Residue |
| A | SER152 |
| A | THR155 |
| A | ILE163 |
| C | PRO204 |
| C | PHE205 |
| C | GLY206 |
| C | GLY207 |
| C | GLY209 |
| C | TRP210 |
| C | ILE212 |
| C | VAL214 |
| C | ASN280 |
| C | ASN281 |
| C | THR282 |
| C | ASP347 |
| C | PHE348 |
| C | ARG349 |
| C | PHE422 |
| C | LMG501 |
| C | HOH608 |
| C | HOH618 |
| site_id | AH5 |
| Number of Residues | 14 |
| Details | binding site for residue SQD C 518 |
| Chain | Residue |
| C | TRP84 |
| C | PRO97 |
| C | LEU104 |
| C | HIS105 |
| C | SER108 |
| C | LEU112 |
| C | LEU161 |
| C | PHE164 |
| C | PHE168 |
| C | PHE169 |
| C | CLA504 |
| C | CLA513 |
| C | CLA514 |
| C | BCR515 |
| site_id | AH6 |
| Number of Residues | 8 |
| Details | binding site for residue BCR C 519 |
| Chain | Residue |
| C | ALA42 |
| C | GLY45 |
| C | LEU46 |
| C | LEU56 |
| C | SER109 |
| C | ALA110 |
| C | CLA512 |
| K | PHE17 |
| site_id | AH7 |
| Number of Residues | 3 |
| Details | binding site for residue CL D 401 |
| Chain | Residue |
| A | ASN181 |
| A | HIS332 |
| D | LYS317 |
| site_id | AH8 |
| Number of Residues | 20 |
| Details | binding site for residue CLA D 402 |
| Chain | Residue |
| A | THR45 |
| A | PHE119 |
| A | MET172 |
| A | ILE176 |
| A | THR179 |
| A | PHE180 |
| A | MET183 |
| A | CLA402 |
| A | PHO404 |
| A | SQD409 |
| A | HOH523 |
| A | HOH535 |
| D | MET198 |
| D | VAL201 |
| D | ALA202 |
| D | CLA405 |
| D | PL9408 |
| D | HOH508 |
| L | LEU32 |
| L | LHG101 |
| site_id | AH9 |
| Number of Residues | 22 |
| Details | binding site for residue PHO D 403 |
| Chain | Residue |
| A | SER209 |
| A | LEU210 |
| A | MET214 |
| A | LEU258 |
| A | CLA403 |
| D | ALA41 |
| D | LEU45 |
| D | TRP48 |
| D | VAL114 |
| D | GLY118 |
| D | GLY121 |
| D | LEU122 |
| D | PHE125 |
| D | GLN129 |
| D | ASN142 |
| D | PHE146 |
| D | PRO149 |
| D | PHE153 |
| D | GLY174 |
| D | ILE204 |
| D | LEU279 |
| D | CLA405 |
| site_id | AI1 |
| Number of Residues | 5 |
| Details | binding site for residue BCT D 404 |
| Chain | Residue |
| A | HIS272 |
| A | FE2401 |
| D | GLU242 |
| D | TYR244 |
| D | HIS268 |
| site_id | AI2 |
| Number of Residues | 23 |
| Details | binding site for residue CLA D 405 |
| Chain | Residue |
| A | MET183 |
| A | PHE206 |
| A | CLA402 |
| A | CLA403 |
| D | LEU122 |
| D | VAL152 |
| D | VAL156 |
| D | PHE181 |
| D | ILE182 |
| D | LEU185 |
| D | GLN186 |
| D | TRP191 |
| D | THR192 |
| D | HIS197 |
| D | GLY200 |
| D | VAL201 |
| D | ILE204 |
| D | LEU279 |
| D | SER282 |
| D | SER283 |
| D | ILE286 |
| D | CLA402 |
| D | PHO403 |
| site_id | AI3 |
| Number of Residues | 15 |
| Details | binding site for residue CLA D 406 |
| Chain | Residue |
| B | CLA608 |
| D | LEU35 |
| D | CYS40 |
| D | LEU89 |
| D | LEU90 |
| D | PHE91 |
| D | LEU92 |
| D | TRP93 |
| D | PHE113 |
| D | HIS117 |
| D | PHE120 |
| H | LEU43 |
| X | LEU12 |
| X | VAL13 |
| X | SQD101 |
| site_id | AI4 |
| Number of Residues | 9 |
| Details | binding site for residue BCR D 407 |
| Chain | Residue |
| D | PHE42 |
| D | MET43 |
| D | GLY47 |
| D | LEU49 |
| D | TRP104 |
| D | LMG412 |
| F | PRO28 |
| F | PHE32 |
| F | VAL33 |
| site_id | AI5 |
| Number of Residues | 20 |
| Details | binding site for residue PL9 D 408 |
| Chain | Residue |
| A | PHE48 |
| A | PHO404 |
| B | CLA607 |
| D | MET198 |
| D | MET199 |
| D | GLY203 |
| D | HIS214 |
| D | THR217 |
| D | TYR244 |
| D | MET246 |
| D | ALA249 |
| D | ASN250 |
| D | TRP253 |
| D | ALA260 |
| D | PHE261 |
| D | LEU267 |
| D | PHE270 |
| D | CLA402 |
| L | VAL28 |
| L | LHG101 |
| site_id | AI6 |
| Number of Residues | 14 |
| Details | binding site for residue LHG D 409 |
| Chain | Residue |
| B | TYR6 |
| B | ARG7 |
| B | PHE464 |
| B | TRP468 |
| B | CLA611 |
| B | CLA613 |
| D | TYR141 |
| D | ARG265 |
| D | TRP266 |
| D | PHE269 |
| D | THR277 |
| D | TRP280 |
| D | HOH527 |
| L | LHG101 |
| site_id | AI7 |
| Number of Residues | 18 |
| Details | binding site for residue LHG D 410 |
| Chain | Residue |
| A | MET37 |
| A | CLA402 |
| A | PHO404 |
| D | PHE257 |
| D | ILE259 |
| D | ALA260 |
| D | PHE261 |
| D | SER262 |
| D | TRP266 |
| D | PHE270 |
| D | HOH523 |
| L | ASN15 |
| L | THR17 |
| L | TYR20 |
| L | LEU21 |
| T | LEU17 |
| T | ALA20 |
| T | ILE21 |
| site_id | AI8 |
| Number of Residues | 19 |
| Details | binding site for residue LHG D 411 |
| Chain | Residue |
| A | ARG140 |
| A | TRP142 |
| A | ALA146 |
| A | PHE273 |
| A | VAL280 |
| A | ILE281 |
| A | PHE285 |
| A | SQD407 |
| C | PHE20 |
| C | TRP23 |
| C | TRP430 |
| C | ARG434 |
| C | CLA509 |
| D | ALA216 |
| D | GLU219 |
| D | SER229 |
| D | ASN230 |
| D | THR231 |
| D | PHE232 |
| site_id | AI9 |
| Number of Residues | 10 |
| Details | binding site for residue LMG D 412 |
| Chain | Residue |
| D | TYR67 |
| D | GLY70 |
| D | ALA71 |
| D | ASN72 |
| D | PHE73 |
| D | BCR407 |
| F | SER29 |
| F | ILE36 |
| F | GLN40 |
| F | ARG44 |
| site_id | AJ1 |
| Number of Residues | 12 |
| Details | binding site for residue HEM E 101 |
| Chain | Residue |
| E | ILE13 |
| E | ARG18 |
| E | TYR19 |
| E | HIS23 |
| E | THR26 |
| F | ARG18 |
| F | TRP19 |
| F | VAL22 |
| F | HIS23 |
| F | ALA26 |
| F | VAL27 |
| F | VAL30 |
| site_id | AJ2 |
| Number of Residues | 19 |
| Details | binding site for residue DGD H 101 |
| Chain | Residue |
| B | PHE193 |
| B | PHE250 |
| B | TYR258 |
| B | TYR273 |
| B | LYS277 |
| B | CLA602 |
| D | HIS87 |
| D | ILE123 |
| D | VAL154 |
| D | MET159 |
| D | LEU162 |
| D | ALA290 |
| D | LEU291 |
| D | HOH502 |
| H | TYR49 |
| H | ASN50 |
| H | VAL60 |
| H | ASP61 |
| H | TRP62 |
| site_id | AJ3 |
| Number of Residues | 7 |
| Details | binding site for residue FME I 101 |
| Chain | Residue |
| A | ILE96 |
| A | TRP97 |
| A | ALA99 |
| I | LEU2 |
| I | THR3 |
| I | LEU4 |
| I | LYS5 |
| site_id | AJ4 |
| Number of Residues | 15 |
| Details | binding site for residue LHG L 101 |
| Chain | Residue |
| B | PRO4 |
| B | TRP5 |
| B | TYR6 |
| B | CLA611 |
| D | ALA202 |
| D | ARG265 |
| D | TRP266 |
| D | PHE273 |
| D | CLA402 |
| D | PL9408 |
| D | LHG409 |
| L | GLU13 |
| L | LEU14 |
| L | SER18 |
| L | LEU21 |
| site_id | AJ5 |
| Number of Residues | 5 |
| Details | binding site for residue FME M 101 |
| Chain | Residue |
| A | GLY74 |
| D | ARG304 |
| M | GLN2 |
| M | VAL3 |
| T | GLU2 |
| site_id | AJ6 |
| Number of Residues | 9 |
| Details | binding site for residue SQD T 101 |
| Chain | Residue |
| L | ARG16 |
| L | LEU19 |
| L | TYR20 |
| L | LEU23 |
| T | LEU8 |
| T | MET12 |
| T | ALA15 |
| T | PHE19 |
| T | PHE23 |
| site_id | AJ7 |
| Number of Residues | 4 |
| Details | binding site for residue FME T 102 |
| Chain | Residue |
| M | PHE8 |
| T | GLU2 |
| T | SER3 |
| T | VAL4 |
| site_id | AJ8 |
| Number of Residues | 4 |
| Details | binding site for residue SQD T 103 |
| Chain | Residue |
| A | ARG27 |
| A | SQD409 |
| T | PHE18 |
| T | PHE23 |
| site_id | AJ9 |
| Number of Residues | 9 |
| Details | binding site for residue SQD X 101 |
| Chain | Residue |
| D | TRP93 |
| D | GLN98 |
| D | GLY99 |
| D | CLA406 |
| X | ASN7 |
| X | TRP10 |
| X | LEU14 |
| X | GLY15 |
| X | ILE18 |
| site_id | AK1 |
| Number of Residues | 7 |
| Details | binding site for residue BCR X 102 |
| Chain | Residue |
| B | CLA601 |
| B | CLA609 |
| H | PHE34 |
| H | LEU37 |
| H | PHE38 |
| H | LEU55 |
| X | LEU5 |
Functional Information from PROSITE/UniProt
| site_id | PS00244 |
| Number of Residues | 27 |
| Details | REACTION_CENTER Photosynthetic reaction center proteins signature. NwtlnPfHmmGvagilggallcAiHGA |
| Chain | Residue | Details |
| D | ASN190-ALA216 | |
| A | ASN191-SER217 |
| site_id | PS00537 |
| Number of Residues | 15 |
| Details | CYTOCHROME_B559 Cytochrome b559 subunits heme-binding site signature. IfTVRWlaVHTLAVP |
| Chain | Residue | Details |
| F | ILE14-PRO28 | |
| E | VAL14-PRO28 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 663 |
| Details | Transmembrane: {"description":"Helical","evidences":[{"source":"PubMed","id":"34937700","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7N8O","evidenceCode":"ECO:0000312"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 606 |
| Details | Topological domain: {"description":"Lumenal, thylakoid","evidences":[{"source":"PubMed","id":"34937700","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7N8O","evidenceCode":"ECO:0000312"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 164 |
| Details | Topological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"34937700","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7N8O","evidenceCode":"ECO:0000312"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Binding site: {"description":"axial binding residue","evidences":[{"source":"HAMAP-Rule","id":"MF_01379","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"34937700","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7N8O","evidenceCode":"ECO:0000312"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 7 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01379","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"34937700","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7N8O","evidenceCode":"ECO:0000312"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"34937700","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7N8O","evidenceCode":"ECO:0000312"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01379","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 1 |
| Details | Site: {"description":"Tyrosine radical intermediate","evidences":[{"source":"HAMAP-Rule","id":"MF_01379","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 1 |
| Details | Site: {"description":"Stabilizes free radical intermediate","evidences":[{"source":"HAMAP-Rule","id":"MF_01379","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 2 |
| Details | Binding site: {"description":"axial binding residue","evidences":[{"source":"HAMAP-Rule","id":"MF_01383","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"34937700","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7N8O","evidenceCode":"ECO:0000312"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 5 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01383","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"34937700","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7N8O","evidenceCode":"ECO:0000312"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI12 |
| Number of Residues | 1 |
| Details | Binding site: {"description":"axial binding residue","evidences":[{"source":"HAMAP-Rule","id":"MF_00642","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"34937700","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"1904816","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"7N8O","evidenceCode":"ECO:0000312"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI13 |
| Number of Residues | 1 |
| Details | Binding site: {"description":"axial binding residue","evidences":[{"source":"HAMAP-Rule","id":"MF_00643","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"34937700","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"1904816","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"7N8O","evidenceCode":"ECO:0000312"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI14 |
| Number of Residues | 20 |
| Details | Transmembrane: {"description":"Helical","evidences":[{"source":"HAMAP-Rule","id":"MF_00808","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"34937700","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7N8O","evidenceCode":"ECO:0000312"}]} |
| Chain | Residue | Details |
