2B11
Crystal structure of the protein-protein complex between F82W cytochrome c and cytochrome c peroxidase
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004601 | molecular_function | peroxidase activity |
| A | 0006979 | biological_process | response to oxidative stress |
| A | 0020037 | molecular_function | heme binding |
| A | 0034599 | biological_process | cellular response to oxidative stress |
| 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 | 0046872 | molecular_function | metal ion binding |
| B | 1901612 | molecular_function | cardiolipin binding |
| C | 0004601 | molecular_function | peroxidase activity |
| C | 0006979 | biological_process | response to oxidative stress |
| C | 0020037 | molecular_function | heme binding |
| C | 0034599 | biological_process | cellular response to oxidative stress |
| D | 0005515 | molecular_function | protein binding |
| D | 0005739 | cellular_component | mitochondrion |
| D | 0005758 | cellular_component | mitochondrial intermembrane space |
| D | 0006122 | biological_process | mitochondrial electron transport, ubiquinol to cytochrome c |
| D | 0006123 | biological_process | mitochondrial electron transport, cytochrome c to oxygen |
| D | 0009055 | molecular_function | electron transfer activity |
| D | 0020037 | molecular_function | heme binding |
| D | 0046872 | molecular_function | metal ion binding |
| D | 1901612 | molecular_function | cardiolipin binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE ZNH A 1001 |
| Chain | Residue |
| A | PRO44 |
| A | LYS179 |
| A | THR180 |
| A | HIS181 |
| A | ASN184 |
| A | SER185 |
| A | TRP191 |
| A | PHE266 |
| A | HOH1401 |
| A | HOH1562 |
| A | HOH1716 |
| A | VAL45 |
| A | VAL47 |
| A | TRP51 |
| A | ASP146 |
| A | LEU171 |
| A | ALA174 |
| A | HIS175 |
| A | GLY178 |
| site_id | AC2 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE HEC C 1201 |
| Chain | Residue |
| C | PRO544 |
| C | TRP551 |
| C | PRO645 |
| C | ASP646 |
| C | LEU671 |
| C | MET672 |
| C | ALA674 |
| C | HIS675 |
| C | GLY678 |
| C | LYS679 |
| C | HIS681 |
| C | ASN684 |
| C | SER685 |
| C | TRP691 |
| C | LEU732 |
| C | THR734 |
| C | HOH1402 |
| C | HOH1433 |
| C | HOH1878 |
| site_id | AC3 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE ZNH B 1101 |
| Chain | Residue |
| A | HOH1841 |
| B | ARG313 |
| B | CYS314 |
| B | CYS317 |
| B | HIS318 |
| B | VAL328 |
| B | ILE335 |
| B | SER340 |
| B | GLY341 |
| B | TYR346 |
| B | TYR348 |
| B | THR349 |
| B | ASN352 |
| B | TRP359 |
| B | MET364 |
| B | TYR367 |
| B | LEU368 |
| B | THR378 |
| B | LYS379 |
| B | MET380 |
| B | ALA381 |
| B | TRP382 |
| B | LEU394 |
| B | HOH1840 |
| B | HOH2444 |
| site_id | AC4 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE HEC D 1301 |
| Chain | Residue |
| D | ARG813 |
| D | CYS814 |
| D | CYS817 |
| D | HIS818 |
| D | VAL828 |
| D | ARG838 |
| D | SER840 |
| D | GLY841 |
| D | TYR846 |
| D | TYR848 |
| D | THR849 |
| D | ASN852 |
| D | TRP859 |
| D | MET864 |
| D | THR878 |
| D | LYS879 |
| D | MET880 |
| D | TRP882 |
| D | LEU894 |
| D | HOH1426 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | BINDING: covalent => ECO:0000269|PubMed:11880631, ECO:0000269|PubMed:18390544, ECO:0007744|PDB:1KYO, ECO:0007744|PDB:3CX5 |
| Chain | Residue | Details |
| B | LEU315 | |
| B | HIS318 | |
| D | LEU815 | |
| D | HIS818 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | BINDING: axial binding residue => ECO:0000269|PubMed:11880631, ECO:0000269|PubMed:18390544, ECO:0007744|PDB:1KYO, ECO:0007744|PDB:3CX5 |
| Chain | Residue | Details |
| B | THR319 | |
| B | ALA381 | |
| D | THR819 | |
| D | ALA881 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | MOD_RES: N6,N6,N6-trimethyllysine; by CTM1 => ECO:0000269|PubMed:10791961, ECO:0000269|PubMed:11880631, ECO:0007744|PDB:1KYO |
| Chain | Residue | Details |
| B | LYS373 | |
| D | LYS873 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | MOD_RES: N6,N6,N6-trimethyllysine => ECO:0000269|PubMed:10821864, ECO:0000269|PubMed:18390544 |
| Chain | Residue | Details |
| B | TYR374 | |
| D | TYR874 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphotyrosine => ECO:0007744|PubMed:18407956 |
| Chain | Residue | Details |
| A | TYR153 | |
| C | TYR653 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1apx |
| Chain | Residue | Details |
| A | ARG48 | |
| A | HIS52 | |
| A | ASN82 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1apx |
| Chain | Residue | Details |
| C | ASN582 | |
| C | ARG548 | |
| C | HIS552 |
| site_id | MCSA1 |
| Number of Residues | 3 |
| Details | M-CSA 709 |
| Chain | Residue | Details |
| A | ARG48 | electrostatic stabiliser |
| A | HIS52 | electrostatic stabiliser, proton acceptor, proton donor |
| A | TRP191 | single electron acceptor, single electron donor |
| site_id | MCSA2 |
| Number of Residues | 3 |
| Details | M-CSA 709 |
| Chain | Residue | Details |
| C | ARG548 | electrostatic stabiliser |
| C | HIS552 | electrostatic stabiliser, proton acceptor, proton donor |
| C | TRP691 | single electron acceptor, single electron donor |
