4LJI
Crystal structure at 1.5 angstrom resolution of the PsbV2 cytochrome from the cyanobacterium thermosynechococcus elongatus
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 | 0009579 | cellular_component | thylakoid |
| A | 0015979 | biological_process | photosynthesis |
| A | 0016020 | cellular_component | membrane |
| A | 0020037 | molecular_function | heme binding |
| A | 0022904 | biological_process | respiratory electron transport chain |
| A | 0031676 | cellular_component | plasma membrane-derived thylakoid membrane |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0005506 | molecular_function | iron ion binding |
| B | 0009055 | molecular_function | electron transfer activity |
| B | 0009523 | cellular_component | photosystem II |
| B | 0009579 | cellular_component | thylakoid |
| B | 0015979 | biological_process | photosynthesis |
| B | 0016020 | cellular_component | membrane |
| B | 0020037 | molecular_function | heme binding |
| B | 0022904 | biological_process | respiratory electron transport chain |
| B | 0031676 | cellular_component | plasma membrane-derived thylakoid membrane |
| B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE HEM A 301 |
| Chain | Residue |
| A | ASN46 |
| A | ARG76 |
| A | LEU82 |
| A | PHE85 |
| A | GLN86 |
| A | TYR92 |
| A | SER98 |
| A | SER100 |
| A | CYS101 |
| A | ARG102 |
| A | ILE121 |
| A | CYS47 |
| A | HOH401 |
| A | HOH404 |
| B | ASN49 |
| A | CYS50 |
| A | HIS51 |
| A | THR56 |
| A | VAL62 |
| A | SER63 |
| A | LEU64 |
| A | ASP68 |
| site_id | AC2 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL A 302 |
| Chain | Residue |
| A | ASN46 |
| A | ARG102 |
| site_id | AC3 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE HEM B 301 |
| Chain | Residue |
| B | ASN46 |
| B | CYS47 |
| B | CYS50 |
| B | HIS51 |
| B | THR56 |
| B | VAL62 |
| B | SER63 |
| B | LEU64 |
| B | ASP68 |
| B | LEU69 |
| B | ALA72 |
| B | ARG76 |
| B | LEU82 |
| B | PHE85 |
| B | GLN86 |
| B | TYR92 |
| B | SER98 |
| B | SER100 |
| B | CYS101 |
| B | ARG102 |
| B | ILE121 |
| B | HOH401 |
| B | HOH402 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Binding site: {"description":"covalent","evidences":[{"source":"PROSITE-ProRule","id":"PRU00433","evidenceCode":"ECO:0000255"},{"source":"PDB","id":"4LJI","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Binding site: {"description":"axial binding residue","evidences":[{"source":"PROSITE-ProRule","id":"PRU00433","evidenceCode":"ECO:0000255"},{"source":"PDB","id":"4LJI","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Binding site: {"description":"axial binding residue","evidences":[{"source":"PDB","id":"4LJI","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
