4N0K
Atomic resolution crystal structure of a cytochrome c-calixarene complex
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 | 24 |
| Details | BINDING SITE FOR RESIDUE HEC A 201 |
| Chain | Residue |
| A | GLU13 |
| A | TYR46 |
| A | TYR48 |
| A | THR49 |
| A | ASN52 |
| A | TRP59 |
| A | MET64 |
| A | TYR67 |
| A | THR78 |
| A | LYS79 |
| A | MET80 |
| A | CYS14 |
| A | PHE82 |
| A | LEU94 |
| A | HOH303 |
| A | HOH343 |
| A | HOH412 |
| A | CYS17 |
| A | HIS18 |
| A | VAL28 |
| A | PRO30 |
| A | ILE35 |
| A | SER40 |
| A | GLY41 |
| site_id | AC2 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE T3Y A 202 |
| 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 | HOH315 |
| A | HOH325 |
| A | HOH339 |
| A | HOH341 |
| A | HOH360 |
| A | HOH366 |
| A | HOH376 |
| A | HOH387 |
| A | HOH392 |
| A | HOH409 |
| A | HOH444 |
| A | HOH446 |
| A | HOH451 |
| site_id | AC3 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE HEC B 201 |
| Chain | Residue |
| B | GLU13 |
| 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 | HOH302 |
| B | HOH364 |
| site_id | AC4 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE T3Y B 202 |
| Chain | Residue |
| A | ASP50 |
| A | LYS54 |
| B | SER2 |
| B | ALA3 |
| B | LYS4 |
| B | LYS5 |
| B | ASN70 |
| B | LYS72 |
| B | LYS73 |
| B | HOH310 |
| B | HOH327 |
| B | HOH333 |
| B | HOH341 |
| B | HOH342 |
| B | HOH357 |
| B | HOH366 |
| B | HOH395 |
| B | HOH438 |
| B | HOH458 |
| site_id | AC5 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE T3Y B 203 |
| Chain | Residue |
| B | GLU88 |
| B | LYS89 |
| B | ASN92 |
| B | GLU103 |
| B | HOH308 |
| B | HOH330 |
| B | HOH332 |
| B | HOH379 |
| B | HOH388 |
| B | HOH402 |
| B | HOH417 |
| B | HOH434 |
| B | HOH474 |
| B | LYS-2 |
| B | LYS22 |
| B | GLY23 |
| B | VAL28 |
| B | HIS33 |
| B | LYS79 |
| B | LYS87 |
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 |
