3O20
Electron transfer complexes:experimental mapping of the Redox-dependent Cytochrome C electrostatic surface
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005515 | molecular_function | protein binding |
| 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 | 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 |
| B | 0005515 | molecular_function | protein binding |
| B | 0005758 | cellular_component | mitochondrial intermembrane space |
| B | 0005829 | cellular_component | cytosol |
| B | 0006122 | biological_process | mitochondrial electron transport, ubiquinol to cytochrome c |
| B | 0006123 | biological_process | mitochondrial electron transport, cytochrome c to oxygen |
| B | 0006915 | biological_process | apoptotic process |
| B | 0008289 | molecular_function | lipid binding |
| B | 0009055 | molecular_function | electron transfer activity |
| B | 0020037 | molecular_function | heme binding |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0070069 | cellular_component | cytochrome complex |
| B | 0097190 | biological_process | apoptotic signaling pathway |
| C | 0005515 | molecular_function | protein binding |
| C | 0005758 | cellular_component | mitochondrial intermembrane space |
| C | 0005829 | cellular_component | cytosol |
| C | 0006122 | biological_process | mitochondrial electron transport, ubiquinol to cytochrome c |
| C | 0006123 | biological_process | mitochondrial electron transport, cytochrome c to oxygen |
| C | 0006915 | biological_process | apoptotic process |
| C | 0008289 | molecular_function | lipid binding |
| C | 0009055 | molecular_function | electron transfer activity |
| C | 0020037 | molecular_function | heme binding |
| C | 0042802 | molecular_function | identical protein binding |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0070069 | cellular_component | cytochrome complex |
| C | 0097190 | biological_process | apoptotic signaling pathway |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE HEC A 105 |
| Chain | Residue |
| A | LYS13 |
| A | TYR48 |
| A | THR49 |
| A | ASN52 |
| A | TRP59 |
| A | LEU64 |
| A | TYR67 |
| A | LEU68 |
| A | THR78 |
| A | LYS79 |
| A | MET80 |
| A | CYS14 |
| A | ILE81 |
| A | PHE82 |
| A | LEU94 |
| A | HOH131 |
| A | HOH211 |
| A | CYS17 |
| A | HIS18 |
| A | THR28 |
| A | GLY29 |
| A | PRO30 |
| A | THR40 |
| A | GLY41 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NO3 A 106 |
| Chain | Residue |
| A | VAL11 |
| A | HOH141 |
| A | HOH168 |
| C | PHE82 |
| C | ALA83 |
| C | GLY84 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE NO3 A 107 |
| Chain | Residue |
| A | PHE82 |
| A | ALA83 |
| A | GLY84 |
| A | HOH179 |
| B | LYS8 |
| B | VAL11 |
| B | GLN12 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NO3 A 108 |
| Chain | Residue |
| A | LYS13 |
| A | GLY84 |
| A | LYS86 |
| A | LYS87 |
| A | GLU90 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE NO3 A 109 |
| Chain | Residue |
| A | THR19 |
| A | VAL20 |
| A | GLU21 |
| A | HOH236 |
| C | THR28 |
| C | ILE81 |
| C | HOH124 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE NO3 A 110 |
| Chain | Residue |
| A | THR28 |
| A | ILE81 |
| A | HOH178 |
| B | PHE10 |
| B | THR19 |
| B | VAL20 |
| B | GLU21 |
| site_id | AC7 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE NO3 A 111 |
| Chain | Residue |
| A | GLY77 |
| A | HOH132 |
| A | HOH261 |
| C | LYS39 |
| C | ILE57 |
| C | THR58 |
| C | LYS60 |
| C | THR63 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NO3 A 112 |
| Chain | Residue |
| A | GLY45 |
| A | PHE46 |
| A | THR47 |
| A | HOH118 |
| A | HOH180 |
| B | LYS53 |
| site_id | AC9 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE HEC B 105 |
| Chain | Residue |
| B | LYS13 |
| B | CYS14 |
| B | GLN16 |
| B | CYS17 |
| B | HIS18 |
| B | THR28 |
| B | GLY29 |
| B | PRO30 |
| B | THR40 |
| B | GLY41 |
| B | TYR48 |
| B | THR49 |
| B | ASN52 |
| B | TRP59 |
| B | LEU64 |
| B | TYR67 |
| B | LEU68 |
| B | THR78 |
| B | LYS79 |
| B | MET80 |
| B | ILE81 |
| B | PHE82 |
| B | LEU94 |
| B | HOH119 |
| B | HOH135 |
| site_id | BC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE NO3 B 106 |
| Chain | Residue |
| B | THR47 |
| B | HOH276 |
| C | LYS25 |
| A | LYS53 |
| B | HIS26 |
| B | GLY45 |
| B | PHE46 |
| site_id | BC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NO3 B 107 |
| Chain | Residue |
| B | LYS27 |
| B | THR28 |
| B | NO3111 |
| C | LYS25 |
| C | LYS27 |
| site_id | BC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NO3 B 108 |
| Chain | Residue |
| B | PHE82 |
| B | ALA83 |
| B | GLY84 |
| B | HOH147 |
| B | HOH332 |
| C | VAL11 |
| site_id | BC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NO3 B 109 |
| Chain | Residue |
| B | LYS13 |
| B | GLY84 |
| B | ILE85 |
| B | LYS86 |
| B | HOH163 |
| C | LYS8 |
| site_id | BC5 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE NO3 B 110 |
| Chain | Residue |
| B | LYS39 |
| B | GLY56 |
| B | ILE57 |
| B | THR58 |
| B | LYS60 |
| B | THR63 |
| B | HOH194 |
| B | HOH355 |
| C | GLY77 |
| C | HOH196 |
| site_id | BC6 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE NO3 B 111 |
| Chain | Residue |
| A | LYS25 |
| A | HIS26 |
| A | LYS27 |
| A | THR28 |
| A | HOH347 |
| B | LYS25 |
| B | LYS27 |
| B | NO3107 |
| B | HOH133 |
| site_id | BC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NO3 B 112 |
| Chain | Residue |
| A | LYS100 |
| B | PHE36 |
| B | LYS60 |
| B | GLU61 |
| B | LYS99 |
| B | HOH136 |
| site_id | BC8 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE NO3 B 113 |
| Chain | Residue |
| A | LYS39 |
| A | GLY56 |
| A | ILE57 |
| A | THR58 |
| A | LYS60 |
| A | HOH142 |
| B | GLY77 |
| B | HOH263 |
| B | HOH354 |
| site_id | BC9 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE HEC C 105 |
| Chain | Residue |
| A | ALA15 |
| C | LYS13 |
| C | CYS14 |
| C | CYS17 |
| C | HIS18 |
| C | THR28 |
| C | GLY29 |
| C | PRO30 |
| C | THR40 |
| C | GLY41 |
| C | PHE46 |
| C | TYR48 |
| C | THR49 |
| C | ASN52 |
| C | TRP59 |
| C | TYR67 |
| C | LEU68 |
| C | THR78 |
| C | LYS79 |
| C | MET80 |
| C | ILE81 |
| C | PHE82 |
| C | LEU98 |
| C | HOH121 |
| C | HOH124 |
| C | HOH136 |
| site_id | CC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE NO3 C 106 |
| Chain | Residue |
| A | GLU4 |
| A | LYS7 |
| C | LYS72 |
| C | ALA83 |
| site_id | CC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE NO3 C 107 |
| Chain | Residue |
| B | THR28 |
| B | ILE81 |
| C | THR19 |
| C | VAL20 |
| C | GLU21 |
| C | HOH117 |
| C | HOH318 |
| site_id | CC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE NO3 C 108 |
| Chain | Residue |
| A | LYS8 |
| A | HOH351 |
| C | LYS13 |
| C | GLY84 |
| C | ILE85 |
| C | LYS86 |
| C | HOH345 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| Details | Binding site: {"description":"covalent"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 3 |
| 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 | 3 |
| Details | Binding site: {"description":"axial binding residue"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 3 |
| 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 | 6 |
| Details | Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P62894","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 3 |
| 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 | 3 |
| 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 | 3 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P62897","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
