9BPB
Tethered respiratory III2IV2 supercomplex from Saccharomyces cerevisiae
Functional Information from PROSITE/UniProt
| site_id | PS00077 |
| Number of Residues | 55 |
| Details | COX1_CUB Heme-copper oxidase catalytic subunit, copper B binding region signature. WFFGHPeVyiliipgfgiishvvstyskkpvfgeismvyamasigllgflvws..HH |
| Chain | Residue | Details |
| m | TRP237-HIS291 |
| site_id | PS00078 |
| Number of Residues | 49 |
| Details | COX2 CO II and nitrous oxide reductase dinuclear copper centers signature. ViHdfaipslgikvdatpgrlnqvsaliqregvfyga......CselCgtgHanM |
| Chain | Residue | Details |
| n | VAL184-MET232 |
| site_id | PS00143 |
| Number of Residues | 23 |
| Details | INSULINASE Insulinase family, zinc-binding region signature. Ggsryatkd.GvAHLLNRFnFqNT |
| Chain | Residue | Details |
| B | GLY37-THR59 |
| site_id | PS00848 |
| Number of Residues | 23 |
| Details | COX5B_1 Cytochrome c oxidase subunit Vb, zinc binding region signature. IMWlkptvnevarCweCGsvYKL |
| Chain | Residue | Details |
| p | ILE121-LEU143 |
| site_id | PS01329 |
| Number of Residues | 18 |
| Details | COX6A Cytochrome c oxidase subunit VIa signature. IRsKpFfWGDGdKTlFwN |
| Chain | Residue | Details |
| w | ILE101-ASN118 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 94 |
| Details | TOPO_DOM: Mitochondrial matrix => ECO:0000269|PubMed:18390544, ECO:0000269|PubMed:30598554 |
| Chain | Residue | Details |
| H | GLY2-PHE49 | |
| M | ILE365-LYS385 | |
| m | LYS264-GLY269 | |
| m | HIS328-ALA335 | |
| m | LEU401-ASN406 | |
| m | GLN475-SER534 | |
| R | GLY2-PHE49 | |
| C | GLY205-SER223 | |
| C | ASP309-LYS319 | |
| C | ILE365-LYS385 | |
| M | MET1-ASN27 | |
| M | TYR103-ARG110 | |
| M | GLY205-SER223 | |
| M | ASP309-LYS319 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 60 |
| Details | TRANSMEM: Helical => ECO:0000269|PubMed:18390544, ECO:0000269|PubMed:30598554 |
| Chain | Residue | Details |
| H | ARG50-LEU80 | |
| M | GLY75-TYR102 | |
| M | VAL111-VAL135 | |
| M | ASN173-HIS204 | |
| M | TYR224-TYR246 | |
| M | LYS288-THR308 | |
| M | VAL320-GLY340 | |
| M | TYR348-LEU364 | |
| R | ARG50-LEU80 | |
| C | VAL111-VAL135 | |
| C | ASN173-HIS204 | |
| C | TYR224-TYR246 | |
| C | LYS288-THR308 | |
| C | VAL320-GLY340 | |
| C | TYR348-LEU364 | |
| M | TYR28-ALA51 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 26 |
| Details | TOPO_DOM: Mitochondrial intermembrane => ECO:0000269|PubMed:18390544, ECO:0000269|PubMed:30598554 |
| Chain | Residue | Details |
| H | TYR81-VAL94 | |
| m | GLY296-ASP298 | |
| m | ALA359-THR370 | |
| m | GLY432-GLY449 | |
| R | TYR81-VAL94 | |
| C | SER247-ASP287 | |
| C | ALA341-PRO347 | |
| M | MET52-ASN74 | |
| M | TYR136-SER172 | |
| M | SER247-ASP287 | |
| M | ALA341-PRO347 | |
| m | PHE216-ASP228 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:10873857, ECO:0000269|PubMed:11880631, ECO:0000269|PubMed:18390544, ECO:0000269|PubMed:30598554, ECO:0007744|PDB:1EZV, ECO:0007744|PDB:1KB9, ECO:0007744|PDB:1KYO, ECO:0007744|PDB:1P84, ECO:0007744|PDB:2IBZ, ECO:0007744|PDB:3CX5, ECO:0007744|PDB:3CXH, ECO:0007744|PDB:4PD4 |
| Chain | Residue | Details |
| E | CYS159 | |
| E | HIS161 | |
| E | CYS178 | |
| E | HIS181 | |
| O | CYS159 | |
| O | HIS161 | |
| O | CYS178 | |
| O | HIS181 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | BINDING: axial binding residue => ECO:0000269|PubMed:11880631, ECO:0000269|PubMed:18390544, ECO:0000269|PubMed:30598554, ECO:0007744|PDB:1KYO |
| Chain | Residue | Details |
| D | HIS105 | |
| N | HIS105 | |
| C | HIS183 | |
| C | HIS197 | |
| M | HIS82 | |
| M | HIS96 | |
| M | HIS183 | |
| M | HIS197 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | BINDING: axial binding residue => ECO:0000269|PubMed:10873857, ECO:0000269|PubMed:11880631, ECO:0000269|PubMed:18390544, ECO:0000269|PubMed:30598554, ECO:0007744|PDB:1EZV, ECO:0007744|PDB:1KYO |
| Chain | Residue | Details |
| D | MET225 | |
| N | MET225 | |
| n | GLU223 | |
| n | HIS229 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 46 |
| Details | TRANSMEM: Helical; Name=5 => ECO:0000269|PubMed:30598554 |
| Chain | Residue | Details |
| c | ASN165-GLU188 | |
| o | ASN165-GLU188 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 56 |
| Details | TRANSMEM: Helical; Name=6 => ECO:0000269|PubMed:30598554 |
| Chain | Residue | Details |
| c | GLY202-MET230 | |
| o | GLY202-MET230 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 32 |
| Details | TRANSMEM: Helical; Name=7 => ECO:0000269|PubMed:30598554 |
| Chain | Residue | Details |
| c | TYR249-TYR265 | |
| o | TYR249-TYR265 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 56 |
| Details | TRANSMEM: Helical; Name=8 => ECO:0000269|PubMed:30598554 |
| Chain | Residue | Details |
| a | ALA299-ILE327 | |
| m | ALA299-ILE327 |
| site_id | SWS_FT_FI11 |
| Number of Residues | 44 |
| Details | TRANSMEM: Helical; Name=9 => ECO:0000269|PubMed:30598554 |
| Chain | Residue | Details |
| a | THR336-LEU358 | |
| m | THR336-LEU358 |
| site_id | SWS_FT_FI12 |
| Number of Residues | 58 |
| Details | TRANSMEM: Helical; Name=10 => ECO:0000269|PubMed:30598554 |
| Chain | Residue | Details |
| a | TYR371-ILE400 | |
| m | TYR371-ILE400 |
| site_id | SWS_FT_FI13 |
| Number of Residues | 48 |
| Details | TRANSMEM: Helical; Name=11 => ECO:0000269|PubMed:30598554 |
| Chain | Residue | Details |
| a | GLU407-LEU431 | |
| m | GLU407-LEU431 |
| site_id | SWS_FT_FI14 |
| Number of Residues | 48 |
| Details | TRANSMEM: Helical; Name=12 => ECO:0000269|PubMed:30598554 |
| Chain | Residue | Details |
| a | TRP450-ASP474 | |
| m | TRP450-ASP474 |
| site_id | SWS_FT_FI15 |
| Number of Residues | 18 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:30598554, ECO:0000269|PubMed:30598556 |
| Chain | Residue | Details |
| a | GLU39 | |
| m | GLU39 | |
| m | ALA42 | |
| m | GLY44 | |
| m | HIS241 | |
| m | HIS290 | |
| m | HIS291 | |
| m | HIS368 | |
| m | ASP369 | |
| m | PRO441 | |
| a | ALA42 | |
| a | GLY44 | |
| a | HIS241 | |
| a | HIS290 | |
| a | HIS291 | |
| a | HIS368 | |
| a | ASP369 | |
| a | PRO441 |
| site_id | SWS_FT_FI16 |
| Number of Residues | 4 |
| Details | BINDING: axial binding residue => ECO:0000269|PubMed:30598554, ECO:0000269|PubMed:30598556 |
| Chain | Residue | Details |
| a | HIS62 | |
| a | HIS378 | |
| m | HIS62 | |
| m | HIS378 |
| site_id | SWS_FT_FI17 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:P00396 |
| Chain | Residue | Details |
| a | TYR245 | |
| m | TYR245 |
| site_id | SWS_FT_FI18 |
| Number of Residues | 2 |
| Details | BINDING: axial binding residue => ECO:0000269|PubMed:30598554 |
| Chain | Residue | Details |
| a | HIS376 | |
| m | HIS376 |
| site_id | SWS_FT_FI19 |
| Number of Residues | 4 |
| Details | CROSSLNK: 1'-histidyl-3'-tyrosine (His-Tyr) => ECO:0000269|PubMed:30598554 |
| Chain | Residue | Details |
| a | HIS241 | |
| a | TYR245 | |
| m | HIS241 | |
| m | TYR245 |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 1 |
| Details | M-CSA 208 |
| Chain | Residue | Details |
| E | HIS181 | covalently attached, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, radical stabiliser |
| C | SER206 | electrostatic stabiliser, hydrogen bond donor, radical stabiliser |
| C | LYS228 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, radical stabiliser |
| C | ASP229 | electrostatic stabiliser, hydrogen bond acceptor, radical stabiliser |
| C | GLU272 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, radical stabiliser |
| site_id | MCSA2 |
| Number of Residues | 1 |
| Details | M-CSA 208 |
| Chain | Residue | Details |
