5KKE
Crystal Structure of a Domain-swapped Dimer of Yeast Iso-1-cytochrome c with CYMAL5
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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 23 |
| Details | binding site for residue HEC A 201 |
| Chain | Residue |
| A | ARG13 |
| A | THR49 |
| A | ALA51 |
| A | TRP59 |
| A | TYR67 |
| A | ALA81 |
| A | PHE82 |
| A | GLY83 |
| A | LEU94 |
| A | CM5204 |
| A | HOH320 |
| A | CYS14 |
| A | HOH330 |
| A | HOH331 |
| A | HOH333 |
| A | HOH347 |
| A | CYS17 |
| A | HIS18 |
| A | VAL28 |
| A | ILE35 |
| A | SER40 |
| A | GLY41 |
| A | TYR48 |
| site_id | AC2 |
| Number of Residues | 9 |
| Details | binding site for residue SO4 A 202 |
| Chain | Residue |
| A | SER2 |
| A | ALA3 |
| A | LYS4 |
| A | SER47 |
| A | TYR48 |
| A | ASN52 |
| A | HOH308 |
| A | HOH318 |
| A | HOH352 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | binding site for residue SO4 A 203 |
| Chain | Residue |
| A | PRO76 |
| A | GLY77 |
| A | THR78 |
| A | LYS79 |
| A | MET80 |
| A | LYS86 |
| A | HOH307 |
| A | HOH317 |
| site_id | AC4 |
| Number of Residues | 12 |
| Details | binding site for residue CM5 A 204 |
| Chain | Residue |
| A | TYR48 |
| A | ASN52 |
| A | LYS55 |
| A | GLU66 |
| A | TYR67 |
| A | LYS73 |
| A | TYR74 |
| A | HEC201 |
| A | HOH302 |
| A | HOH302 |
| A | HOH306 |
| A | HOH315 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | binding site for residue GOL A 206 |
| Chain | Residue |
| A | GLY23 |
| A | GLY24 |
| A | HIS26 |
| A | GLY45 |
| A | HOH323 |
| A | HOH324 |
| site_id | AC6 |
| Number of Residues | 1 |
| Details | binding site for residue GOL A 207 |
| Chain | Residue |
| A | PHE82 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| 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 | 2 |
| 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 | 1 |
| 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 | 1 |
| 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 |
