1EWH
STRUCTURE OF CYTOCHROME F FROM CHLAMYDOMONAS REINHARDTII
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005506 | molecular_function | iron ion binding |
| A | 0009055 | molecular_function | electron transfer activity |
| A | 0015979 | biological_process | photosynthesis |
| A | 0020037 | molecular_function | heme binding |
| A | 0042651 | cellular_component | thylakoid membrane |
| B | 0005506 | molecular_function | iron ion binding |
| B | 0009055 | molecular_function | electron transfer activity |
| B | 0015979 | biological_process | photosynthesis |
| B | 0020037 | molecular_function | heme binding |
| B | 0042651 | cellular_component | thylakoid membrane |
| C | 0005506 | molecular_function | iron ion binding |
| C | 0009055 | molecular_function | electron transfer activity |
| C | 0015979 | biological_process | photosynthesis |
| C | 0020037 | molecular_function | heme binding |
| C | 0042651 | cellular_component | thylakoid membrane |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ACT C 801 |
| Chain | Residue |
| A | VAL180 |
| C | VAL44 |
| C | ARG88 |
| C | HOH802 |
| C | HOH812 |
| site_id | AC2 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE HEC A 253 |
| Chain | Residue |
| A | CYS21 |
| A | CYS24 |
| A | HIS25 |
| A | GLN59 |
| A | LEU69 |
| A | ASN70 |
| A | VAL71 |
| A | GLY72 |
| A | MET73 |
| A | ASN153 |
| A | GLY155 |
| A | ARG156 |
| A | GLY157 |
| A | VAL159 |
| A | PRO161 |
| A | HOH298 |
| A | HOH463 |
| C | ASN16 |
| C | HOH860 |
| A | TYR1 |
| A | PHE4 |
| A | ALA5 |
| A | VAL20 |
| site_id | AC3 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE HEC B 253 |
| Chain | Residue |
| A | VAL245 |
| B | TYR1 |
| B | PRO2 |
| B | PHE4 |
| B | CYS21 |
| B | CYS24 |
| B | HIS25 |
| B | GLN59 |
| B | LEU69 |
| B | ASN70 |
| B | VAL71 |
| B | GLY72 |
| B | MET73 |
| B | VAL74 |
| B | ASN153 |
| B | GLY155 |
| B | ARG156 |
| B | GLY157 |
| B | VAL159 |
| B | TYR160 |
| B | HOH271 |
| B | HOH275 |
| B | HOH391 |
| site_id | AC4 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE HEC C 253 |
| Chain | Residue |
| C | TYR1 |
| C | PHE4 |
| C | ALA5 |
| C | CYS21 |
| C | CYS24 |
| C | HIS25 |
| C | GLN59 |
| C | LEU69 |
| C | ASN70 |
| C | VAL71 |
| C | GLY72 |
| C | MET73 |
| C | ASN153 |
| C | GLY155 |
| C | ARG156 |
| C | GLY157 |
| C | VAL159 |
| C | TYR160 |
| C | HOH811 |
| C | HOH863 |
| C | HOH904 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| 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_FI2 |
| Number of Residues | 6 |
| Details | Binding site: {"description":"covalent","evidences":[{"source":"PubMed","id":"10869174","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"10924110","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
