1Q90
Structure of the cytochrome b6f (plastohydroquinone : plastocyanin oxidoreductase) from Chlamydomonas reinhardtii
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005506 | molecular_function | iron ion binding |
| A | 0005515 | molecular_function | protein binding |
| A | 0009055 | molecular_function | electron transfer activity |
| A | 0009535 | cellular_component | chloroplast thylakoid membrane |
| A | 0015979 | biological_process | photosynthesis |
| A | 0020037 | molecular_function | heme binding |
| A | 0042651 | cellular_component | thylakoid membrane |
| B | 0009055 | molecular_function | electron transfer activity |
| B | 0009535 | cellular_component | chloroplast thylakoid membrane |
| B | 0015979 | biological_process | photosynthesis |
| B | 0016020 | cellular_component | membrane |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0022904 | biological_process | respiratory electron transport chain |
| C | 0016020 | cellular_component | membrane |
| C | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
| D | 0009055 | molecular_function | electron transfer activity |
| D | 0009535 | cellular_component | chloroplast thylakoid membrane |
| D | 0009767 | biological_process | photosynthetic electron transport chain |
| D | 0015979 | biological_process | photosynthesis |
| D | 0016020 | cellular_component | membrane |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0042651 | cellular_component | thylakoid membrane |
| G | 0009055 | molecular_function | electron transfer activity |
| G | 0009512 | cellular_component | cytochrome b6f complex |
| G | 0009535 | cellular_component | chloroplast thylakoid membrane |
| G | 0017004 | biological_process | cytochrome complex assembly |
| L | 0009055 | molecular_function | electron transfer activity |
| L | 0009512 | cellular_component | cytochrome b6f complex |
| M | 0009512 | cellular_component | cytochrome b6f complex |
| N | 0009512 | cellular_component | cytochrome b6f complex |
| N | 0017004 | biological_process | cytochrome complex assembly |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE HEC A 900 |
| Chain | Residue |
| A | TYR1 |
| A | LEU69 |
| A | ASN70 |
| A | VAL71 |
| A | GLY72 |
| A | MET73 |
| A | ASN153 |
| A | GLY155 |
| A | ARG156 |
| A | GLY157 |
| A | VAL159 |
| A | PRO2 |
| A | TYR160 |
| A | PRO161 |
| A | PHE4 |
| A | ALA5 |
| A | CYS21 |
| A | CYS24 |
| A | HIS25 |
| A | GLN59 |
| A | ALA62 |
| site_id | AC2 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE HEC B 903 |
| Chain | Residue |
| B | VAL30 |
| B | TYR34 |
| B | CYS35 |
| B | GLY38 |
| B | PHE203 |
| B | ARG207 |
| B | GLY210 |
| B | ILE211 |
| B | HEC901 |
| B | HOH963 |
| D | ASN25 |
| D | PHE40 |
| D | ILE44 |
| site_id | AC3 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE HEC B 901 |
| Chain | Residue |
| B | TYR34 |
| B | GLY37 |
| B | GLY38 |
| B | THR40 |
| B | PHE41 |
| B | HIS100 |
| B | ARG103 |
| B | VAL104 |
| B | GLY109 |
| B | ARG114 |
| B | THR117 |
| B | TRP118 |
| B | GLY121 |
| B | VAL122 |
| B | MET124 |
| B | ALA125 |
| B | HIS202 |
| B | ILE206 |
| B | ILE211 |
| B | SER212 |
| B | HEC903 |
| B | HOH961 |
| B | HOH963 |
| site_id | AC4 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE HEC B 902 |
| Chain | Residue |
| B | GLN47 |
| B | GLY51 |
| B | PHE52 |
| B | MET54 |
| B | ARG83 |
| B | HIS86 |
| B | ARG87 |
| B | ALA90 |
| B | PHE131 |
| B | GLY135 |
| B | TYR136 |
| B | LEU138 |
| B | PRO139 |
| B | HIS187 |
| B | THR188 |
| B | PRO192 |
| site_id | AC5 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE FES C 210 |
| Chain | Residue |
| C | CYS134 |
| C | HIS136 |
| C | LEU137 |
| C | GLY138 |
| C | CYS139 |
| C | CYS152 |
| C | HIS155 |
| C | GLY156 |
| C | SER157 |
| site_id | AC6 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE CLA D 910 |
| Chain | Residue |
| B | TYR105 |
| B | ALA125 |
| B | SER130 |
| B | VAL133 |
| D | TYR80 |
| D | PHE81 |
| D | PRO83 |
| D | VAL104 |
| D | LEU132 |
| D | PHE133 |
| D | GLY136 |
| D | VAL139 |
| D | LMG953 |
| site_id | AC7 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE BCR B 904 |
| Chain | Residue |
| D | THR47 |
| G | VAL16 |
| G | GLY20 |
| G | VAL23 |
| M | THR77 |
| M | LEU81 |
| N | PHE84 |
| B | ILE32 |
| B | PHE33 |
| B | ILE39 |
| B | LEU99 |
| site_id | AC8 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE TDS D 920 |
| Chain | Residue |
| B | ALA147 |
| B | ILE150 |
| B | VAL151 |
| C | CYS154 |
| C | HIS155 |
| D | ILE75 |
| D | LEU76 |
| D | PRO77 |
| D | PHE85 |
| D | LEU88 |
| D | MET101 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SQD R 950 |
| Chain | Residue |
| A | LYS272 |
| A | PHE276 |
| D | TRP32 |
| R | ARG42 |
| R | ASN46 |
| site_id | BC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE LFA B 960 |
| Chain | Residue |
| A | ARG251 |
| A | LEU255 |
| B | LEU81 |
| R | GLY63 |
| R | TYR64 |
| site_id | BC2 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE LMG L 951 |
| Chain | Residue |
| A | GLN37 |
| B | ILE39 |
| B | CYS43 |
| B | MET92 |
| B | MET96 |
| D | THR47 |
| D | CYS50 |
| D | LEU54 |
| L | THR3 |
| L | ILE4 |
| L | TYR7 |
| M | PHE65 |
| M | THR69 |
| M | THR72 |
| M | MET76 |
| N | GLU69 |
| N | GLN74 |
| N | TRP77 |
| site_id | BC3 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE LMG D 953 |
| Chain | Residue |
| B | PHE102 |
| D | LEU134 |
| D | THR137 |
| D | ILE145 |
| D | THR148 |
| D | CLA910 |
| G | CYS7 |
| G | PRO15 |
| G | ILE18 |
| G | PHE22 |
| M | ALA63 |
| M | ILE66 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 61 |
| Details | Transmembrane: {"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Binding site: {"description":"axial binding residue","evidences":[{"source":"PubMed","id":"10869174","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"10924110","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Binding site: {"description":"covalent","evidences":[{"source":"PubMed","id":"10869174","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"10924110","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 80 |
| Details | Transmembrane: {"description":"Helical","evidences":[{"source":"HAMAP-Rule","id":"MF_00633","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | Binding site: {"description":"covalent","evidences":[{"source":"PubMed","id":"14647374","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15049703","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"1Q90","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 7 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"14647374","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1Q90","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 4 |
| Details | Binding site: {"description":"axial binding residue","evidences":[{"source":"PubMed","id":"14647374","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1Q90","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 4 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 60 |
| Details | Transmembrane: {"description":"Helical","evidences":[{"source":"HAMAP-Rule","id":"MF_01344","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 29 |
| Details | Transmembrane: {"description":"Helical"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 20 |
| Details | Transmembrane: {"description":"Helical","evidences":[{"source":"HAMAP-Rule","id":"MF_00432","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI12 |
| Number of Residues | 20 |
| Details | Transmembrane: {"description":"Helical","evidences":[{"source":"HAMAP-Rule","id":"MF_00433","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ndo |
| Chain | Residue | Details |
| C | HIS155 |
