8UGI
High resolution in-situ structure of typeA supercomplex in respiratory chain (I1III2IV1,composite)
This is a non-PDB format compatible entry.
Functional Information from PROSITE/UniProt
| site_id | PS00012 |
| Number of Residues | 16 |
| Details | PHOSPHOPANTETHEINE Phosphopantetheine attachment site. DLGLDSLDQVEIIMAM |
| Chain | Residue | Details |
| 1T | ASP39-MET54 |
| site_id | PS00018 |
| Number of Residues | 13 |
| Details | EF_HAND_1 EF-hand calcium-binding domain. DIDAEKLMCpqEI |
| Chain | Residue | Details |
| 1T | ASP64-ILE76 |
| site_id | PS00077 |
| Number of Residues | 56 |
| Details | COX1_CUB Heme-copper oxidase catalytic subunit, copper B binding region signature. WFFGHPeVyililpgfgmishivtyysgkkepfgymgmvwammsigflgfivwa.HH |
| Chain | Residue | Details |
| 4A | TRP236-HIS291 |
| site_id | PS00078 |
| Number of Residues | 49 |
| Details | COX2 CO II and nitrous oxide reductase dinuclear copper centers signature. VlHswavpslglktdaipgrlnqttlmstrpglyygq......CseiCgsnHsfM |
| Chain | Residue | Details |
| 4B | VAL159-MET207 |
| site_id | PS00143 |
| Number of Residues | 24 |
| Details | INSULINASE Insulinase family, zinc-binding region signature. GsryedsnnlGtSHLLRLAsSlTT |
| Chain | Residue | Details |
| 3O | GLY54-THR77 |
| site_id | PS00198 |
| Number of Residues | 12 |
| Details | 4FE4S_FER_1 4Fe-4S ferredoxin-type iron-sulfur binding region signature. CiACKlCEaVCP |
| Chain | Residue | Details |
| 1I | CYS77-PRO88 | |
| 1I | CYS116-PRO127 |
| site_id | PS00535 |
| Number of Residues | 12 |
| Details | COMPLEX1_49K Respiratory chain NADH dehydrogenase 49 Kd subunit signature. LHRGtEKLiEyK |
| Chain | Residue | Details |
| 1D | LEU83-LYS94 |
| site_id | PS00542 |
| Number of Residues | 22 |
| Details | COMPLEX1_30K Respiratory chain NADH dehydrogenase 30 Kd subunit signature. EREiwDMFgvffanHpdlRrIL |
| Chain | Residue | Details |
| 1C | GLU131-LEU152 |
| site_id | PS00641 |
| Number of Residues | 18 |
| Details | COMPLEX1_75K_1 Respiratory-chain NADH dehydrogenase 75 Kd subunit signature 1. PrfCYherlsvaGnCRmC |
| Chain | Residue | Details |
| 1G | PRO38-CYS55 |
| site_id | PS00642 |
| Number of Residues | 13 |
| Details | COMPLEX1_75K_2 Respiratory-chain NADH dehydrogenase 75 Kd subunit signature 2. CPiCDqGGeCdLQ |
| Chain | Residue | Details |
| 1G | CYS105-GLN117 |
| site_id | PS00643 |
| Number of Residues | 11 |
| Details | COMPLEX1_75K_3 Respiratory-chain NADH dehydrogenase 75 Kd subunit signature 3. RCIqCtRCIrF |
| Chain | Residue | Details |
| 1G | ARG152-PHE162 |
| site_id | PS00644 |
| Number of Residues | 16 |
| Details | COMPLEX1_51K_1 Respiratory-chain NADH dehydrogenase 51 Kd subunit signature 1. GAGAYICGEETALIES |
| Chain | Residue | Details |
| 1F | GLY180-SER195 |
| site_id | PS00645 |
| Number of Residues | 12 |
| Details | COMPLEX1_51K_2 Respiratory-chain NADH dehydrogenase 51 Kd subunit signature 2. ESCGqCtPCReG |
| Chain | Residue | Details |
| 1F | GLU357-GLY368 |
| site_id | PS00667 |
| Number of Residues | 16 |
| Details | COMPLEX1_ND1_1 Respiratory-chain NADH dehydrogenase subunit 1 signature 1. GLLQpIaDALKLVtKE |
| Chain | Residue | Details |
| 1H | GLY44-GLU59 |
| site_id | PS00668 |
| Number of Residues | 14 |
| Details | COMPLEX1_ND1_2 Respiratory-chain NADH dehydrogenase subunit 1 signature 2. PFDLTEGEseLVs.G |
| Chain | Residue | Details |
| 1H | PRO197-GLY210 |
| site_id | PS00848 |
| Number of Residues | 23 |
| Details | COX5B_1 Cytochrome c oxidase subunit Vb, zinc binding region signature. VIWfwvhkgetqrCpsCGthYKL |
| Chain | Residue | Details |
| 4F | VAL69-LEU91 |
| site_id | PS01099 |
| Number of Residues | 19 |
| Details | COMPLEX1_24K Respiratory-chain NADH dehydrogenase 24 Kd subunit signature. DklFTlieveCLGaCvnAP |
| Chain | Residue | Details |
| 1E | ASP134-PRO152 |
| site_id | PS01150 |
| Number of Residues | 17 |
| Details | COMPLEX1_20K Respiratory-chain NADH dehydrogenase 20 Kd subunit signature. GcDRIVPVDIYvPgCPP |
| Chain | Residue | Details |
| 1B | GLY135-PRO151 |
| site_id | PS01329 |
| Number of Residues | 18 |
| Details | COX6A Cytochrome c oxidase subunit VIa signature. IRtKpYsWGDGnHTlFhN |
| Chain | Residue | Details |
| 4G | ILE55-ASN72 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 16 |
| Details | TOPO_DOM: Mitochondrial matrix => ECO:0000250|UniProtKB:P00430 |
| Chain | Residue | Details |
| 4L | SER1-ASN17 | |
| 1N | LEU325-SER345 | |
| 1M | ILE391-THR413 | |
| 1M | ALA435-LEU455 | |
| 1L | TRP407-PHE429 | |
| 1L | LEU457-VAL477 | |
| 1L | MET482-LEU502 | |
| 1L | GLY582-PHE602 | |
| 4F | CYS62 | |
| 4F | CYS82 | |
| 4F | CYS85 | |
| 4A | HIS328-SER335 | |
| 4A | SER401-ASN406 | |
| 4A | LYS479-LYS514 | |
| 1N | MET237-LEU257 | |
| 1N | GLU274-MET294 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 26 |
| Details | TRANSMEM: Helical => ECO:0000250|UniProtKB:P00430 |
| Chain | Residue | Details |
| 4L | LYS18-LEU44 | |
| 4F | LYS55 | |
| 4F | LYS90 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | TOPO_DOM: Mitochondrial intermembrane => ECO:0000250|UniProtKB:P00430 |
| Chain | Residue | Details |
| 4L | LEU45-LYS47 | |
| 4C | LEU106-GLU128 | |
| 4C | ALA184-ASP190 | |
| 4C | TYR257-SER261 | |
| 4A | LEU358-THR370 | |
| 4A | SER434-ALA446 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | MOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P17665 |
| Chain | Residue | Details |
| 4L | LYS9 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 32 |
| Details | TRANSMEM: Helical; Name=III => ECO:0000250|UniProtKB:P00415 |
| Chain | Residue | Details |
| 4C | SER73-SER105 | |
| 4B | CYS196 | |
| 4B | GLU198 | |
| 4B | CYS200 | |
| 4B | HIS204 | |
| 4B | MET207 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 23 |
| Details | TRANSMEM: Helical; Name=IV => ECO:0000250|UniProtKB:P00415 |
| Chain | Residue | Details |
| 4C | VAL129-MET152 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 27 |
| Details | TRANSMEM: Helical; Name=V => ECO:0000250|UniProtKB:P00415 |
| Chain | Residue | Details |
| 4C | ARG156-GLU183 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 32 |
| Details | TRANSMEM: Helical; Name=VI => ECO:0000250|UniProtKB:P00415 |
| Chain | Residue | Details |
| 4C | GLY191-LEU223 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 23 |
| Details | TRANSMEM: Helical; Name=VII => ECO:0000250|UniProtKB:P00415 |
| Chain | Residue | Details |
| 4C | PHE233-ILE256 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 28 |
| Details | TRANSMEM: Helical; Name=VIII => ECO:0000250|UniProtKB:P00396 |
| Chain | Residue | Details |
| 4A | VAL299-LEU327 |
| site_id | SWS_FT_FI11 |
| Number of Residues | 21 |
| Details | TRANSMEM: Helical; Name=IX => ECO:0000250|UniProtKB:P00396 |
| Chain | Residue | Details |
| 4A | PRO336-VAL357 |
| site_id | SWS_FT_FI12 |
| Number of Residues | 29 |
| Details | TRANSMEM: Helical; Name=X => ECO:0000250|UniProtKB:P00396 |
| Chain | Residue | Details |
| 4A | TYR371-PHE400 |
| site_id | SWS_FT_FI13 |
| Number of Residues | 26 |
| Details | TRANSMEM: Helical; Name=XI => ECO:0000250|UniProtKB:P00396 |
| Chain | Residue | Details |
| 4A | GLN407-LEU433 |
| site_id | SWS_FT_FI14 |
| Number of Residues | 31 |
| Details | TRANSMEM: Helical; Name=XII => ECO:0000250|UniProtKB:P00396 |
| Chain | Residue | Details |
| 4A | TYR447-SER478 |
| site_id | SWS_FT_FI15 |
| Number of Residues | 9 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:P00396 |
| Chain | Residue | Details |
| 4A | GLU40 | |
| 4A | GLY45 | |
| 4A | HIS240 | |
| 4A | TYR244 | |
| 4A | HIS290 | |
| 4A | HIS291 | |
| 4A | HIS368 | |
| 4A | ASP369 | |
| 4A | SER441 |
| site_id | SWS_FT_FI16 |
| Number of Residues | 3 |
| Details | BINDING: axial binding residue => ECO:0000250|UniProtKB:P00396 |
| Chain | Residue | Details |
| 4A | HIS61 | |
| 4A | HIS376 | |
| 4A | HIS378 |
| site_id | SWS_FT_FI17 |
| Number of Residues | 2 |
| Details | CROSSLNK: 1'-histidyl-3'-tyrosine (His-Tyr) => ECO:0000250|UniProtKB:P00396 |
| Chain | Residue | Details |
| 4A | HIS240 | |
| 4A | TYR244 |
