3TYI
Crystal Structure of Cytochrome c - p-Sulfonatocalix[4]arene Complexes
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 | 0006122 | biological_process | mitochondrial electron transport, ubiquinol to cytochrome c |
| A | 0006123 | biological_process | mitochondrial electron transport, cytochrome c to oxygen |
| A | 0009055 | molecular_function | electron transfer activity |
| A | 0020037 | molecular_function | heme binding |
| A | 0022904 | biological_process | respiratory electron transport chain |
| A | 0046872 | molecular_function | metal ion binding |
| A | 1901612 | molecular_function | cardiolipin binding |
| B | 0005515 | molecular_function | protein binding |
| B | 0005739 | cellular_component | mitochondrion |
| B | 0005758 | cellular_component | mitochondrial intermembrane space |
| B | 0006122 | biological_process | mitochondrial electron transport, ubiquinol to cytochrome c |
| B | 0006123 | biological_process | mitochondrial electron transport, cytochrome c to oxygen |
| B | 0009055 | molecular_function | electron transfer activity |
| B | 0020037 | molecular_function | heme binding |
| B | 0022904 | biological_process | respiratory electron transport chain |
| B | 0046872 | molecular_function | metal ion binding |
| B | 1901612 | molecular_function | cardiolipin binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE HEM A 104 |
| Chain | Residue |
| A | ARG13 |
| A | GLY41 |
| A | TYR46 |
| A | TYR48 |
| A | THR49 |
| A | ASN52 |
| A | TRP59 |
| A | MET64 |
| A | TYR67 |
| A | THR78 |
| A | LYS79 |
| A | CYS14 |
| A | MET80 |
| A | PHE82 |
| A | HOH172 |
| A | HOH209 |
| A | CYS17 |
| A | HIS18 |
| A | VAL28 |
| A | GLY29 |
| A | PRO30 |
| A | ILE35 |
| A | SER40 |
| site_id | AC2 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE T3Y A 105 |
| Chain | Residue |
| A | LYS-2 |
| A | SER2 |
| A | ALA3 |
| A | LYS4 |
| A | LYS5 |
| A | ALA7 |
| A | LYS87 |
| A | GLU88 |
| A | LYS89 |
| A | ASN92 |
| A | TYR97 |
| A | LYS100 |
| A | HOH109 |
| A | HOH121 |
| A | HOH124 |
| A | HOH125 |
| A | HOH132 |
| A | HOH142 |
| A | HOH149 |
| A | HOH186 |
| A | HOH201 |
| A | HOH206 |
| A | HOH223 |
| A | HOH229 |
| A | HOH236 |
| A | HOH316 |
| site_id | AC3 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE HEM B 104 |
| Chain | Residue |
| B | ARG13 |
| B | CYS14 |
| B | CYS17 |
| B | HIS18 |
| B | VAL28 |
| B | PRO30 |
| B | ILE35 |
| B | SER40 |
| B | GLY41 |
| B | TYR46 |
| B | TYR48 |
| B | THR49 |
| B | ASN52 |
| B | TRP59 |
| B | MET64 |
| B | TYR67 |
| B | LEU68 |
| B | THR78 |
| B | LYS79 |
| B | MET80 |
| B | ALA81 |
| B | PHE82 |
| B | LEU94 |
| B | HOH160 |
| B | HOH181 |
| site_id | AC4 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE T3Y B 105 |
| Chain | Residue |
| A | ASP50 |
| A | LYS54 |
| B | SER2 |
| B | ALA3 |
| B | LYS4 |
| B | LYS5 |
| B | ASN70 |
| B | LYS72 |
| B | LYS73 |
| B | PRO76 |
| B | HOH134 |
| B | HOH167 |
| B | HOH176 |
| B | HOH177 |
| B | HOH190 |
| B | HOH215 |
| B | HOH273 |
| B | HOH283 |
| B | HOH288 |
| B | HOH307 |
| B | HOH389 |
| site_id | AC5 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE T3Y B 106 |
| Chain | Residue |
| B | LYS79 |
| B | LYS87 |
| B | GLU88 |
| B | LYS89 |
| B | ASN92 |
| B | GLU103 |
| B | HOH139 |
| B | HOH146 |
| B | HOH196 |
| B | HOH206 |
| B | HOH249 |
| B | HOH271 |
| B | HOH392 |
| B | LYS22 |
| B | GLY23 |
| B | VAL28 |
| B | HIS33 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Binding site: {"description":"covalent","evidences":[{"source":"PubMed","id":"11880631","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18390544","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1KYO","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3CX5","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Binding site: {"description":"axial binding residue","evidences":[{"source":"PubMed","id":"11880631","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18390544","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1KYO","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3CX5","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6,N6,N6-trimethyllysine; by CTM1","evidences":[{"source":"PubMed","id":"10791961","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11880631","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1KYO","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6,N6,N6-trimethyllysine","evidences":[{"source":"PubMed","id":"10821864","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18390544","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
