1FI9
SOLUTION STRUCTURE OF THE IMIDAZOLE COMPLEX OF CYTOCHROME C
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005515 | molecular_function | protein binding |
| A | 0005739 | cellular_component | mitochondrion |
| A | 0005758 | cellular_component | mitochondrial intermembrane space |
| A | 0005829 | cellular_component | cytosol |
| A | 0006122 | biological_process | mitochondrial electron transport, ubiquinol to cytochrome c |
| A | 0006123 | biological_process | mitochondrial electron transport, cytochrome c to oxygen |
| A | 0006915 | biological_process | apoptotic process |
| A | 0008289 | molecular_function | lipid binding |
| A | 0009055 | molecular_function | electron transfer activity |
| A | 0018063 | biological_process | cytochrome c-heme linkage |
| A | 0020037 | molecular_function | heme binding |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0070069 | cellular_component | cytochrome complex |
| A | 0097190 | biological_process | apoptotic signaling pathway |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE IMD A 105 |
| Chain | Residue |
| A | TYR67 |
| A | LYS79 |
| A | HEC110 |
| site_id | AC2 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE HEC A 110 |
| Chain | Residue |
| A | PRO30 |
| A | LEU32 |
| A | LEU35 |
| A | THR49 |
| A | ASN52 |
| A | TRP59 |
| A | TYR67 |
| A | LEU68 |
| A | LYS79 |
| A | LEU94 |
| A | IMD105 |
| A | LYS13 |
| A | CYS14 |
| A | CYS17 |
| A | HIS18 |
| A | THR28 |
| A | GLY29 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Binding site: {"description":"covalent"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Binding site: {"description":"axial binding residue","evidences":[{"source":"PROSITE-ProRule","id":"PRU00433","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"5545094","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Binding site: {"description":"axial binding residue"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N-acetylglycine","evidences":[{"source":"PubMed","id":"14469771","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P62894","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P62897","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P62897","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P62897","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
