1E2V
N153Q mutant 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 | 3 |
| Details | BINDING SITE FOR RESIDUE ACT A 901 |
| Chain | Residue |
| A | PRO119 |
| A | TYR123 |
| A | HOH2243 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE ACT A 902 |
| Chain | Residue |
| B | GLY463 |
| A | GLN220 |
| A | THR221 |
| A | GLN226 |
| A | HOH2413 |
| B | PRO461 |
| B | ASP462 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ACT B 901 |
| Chain | Residue |
| B | ASN308 |
| B | TYR309 |
| B | ALA310 |
| B | HOH2379 |
| B | HOH2380 |
| site_id | AC4 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE HEC A 900 |
| Chain | Residue |
| A | TYR1 |
| A | PHE4 |
| A | CYS21 |
| A | CYS24 |
| A | HIS25 |
| A | GLN59 |
| A | ALA62 |
| A | LEU69 |
| A | ASN70 |
| A | VAL71 |
| A | GLY72 |
| A | MET73 |
| A | GLN153 |
| A | GLY155 |
| A | ARG156 |
| A | GLY157 |
| A | VAL159 |
| A | TYR160 |
| A | HOH2410 |
| A | HOH2411 |
| A | HOH2412 |
| C | ASN616 |
| C | HOH2134 |
| site_id | AC5 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE HEC B 900 |
| Chain | Residue |
| B | TYR301 |
| B | PRO302 |
| B | PHE304 |
| B | ALA305 |
| B | CYS321 |
| B | CYS324 |
| B | HIS325 |
| B | GLN359 |
| B | LEU369 |
| B | ASN370 |
| B | VAL371 |
| B | GLY372 |
| B | MET373 |
| B | GLN453 |
| B | GLY455 |
| B | ARG456 |
| B | GLY457 |
| B | VAL459 |
| B | TYR460 |
| B | PRO461 |
| B | HOH2376 |
| B | HOH2377 |
| B | HOH2378 |
| site_id | AC6 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE HEC C 900 |
| Chain | Residue |
| C | TYR601 |
| C | PHE604 |
| C | ALA605 |
| C | CYS621 |
| C | CYS624 |
| C | HIS625 |
| C | GLN659 |
| C | LEU669 |
| C | ASN670 |
| C | VAL671 |
| C | GLY672 |
| C | MET673 |
| C | GLN753 |
| C | GLY755 |
| C | ARG756 |
| C | GLY757 |
| C | VAL759 |
| C | TYR760 |
| C | PRO761 |
| C | HOH2391 |
| C | HOH2392 |
| C | HOH2393 |
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 |
