9OCV
Cryo-EM structure of the CIII2CIV1 respiratory supercomplex from Bacillus subtilis
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. WIFGHPeVyililpafgifsevipvfarkrlfgyssmvfaivligflgfmvwv..HH |
| Chain | Residue | Details |
| M | TRP245-HIS299 |
| site_id | PS00078 |
| Number of Residues | 55 |
| Details | COX2 CO II and nitrous oxide reductase dinuclear copper centers signature. VkHsfwipsvggkldtntdnenkffltfdskrskeagdmffgkCaelCgpsHalM |
| Chain | Residue | Details |
| N | VAL174-MET228 |
| site_id | PS00213 |
| Number of Residues | 13 |
| Details | LIPOCALIN Lipocalin signature. EGKn.KFLGFWLFL |
| Chain | Residue | Details |
| L | GLU22-LEU34 |
| site_id | PS00267 |
| Number of Residues | 6 |
| Details | TACHYKININ Tachykinin family signature. FVGLMG |
| Chain | Residue | Details |
| M | PHE438-GLY443 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 198 |
| Details | Domain: {"description":"Rieske","evidences":[{"source":"PROSITE-ProRule","id":"PRU00628","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00628","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 160 |
| Details | Transmembrane: {"description":"Helical","evidences":[{"source":"PROSITE-ProRule","id":"PRU00968","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"Q57038","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Binding site: {"description":"covalent","evidences":[{"source":"UniProtKB","id":"Q57038","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 8 |
| Details | Binding site: {"description":"axial binding residue","evidences":[{"source":"UniProtKB","id":"Q57038","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 112 |
| Details | Transmembrane: {"description":"Helical","evidences":[{"source":"PROSITE-ProRule","id":"PRU00967","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 150 |
| Details | Domain: {"description":"Cytochrome c","evidences":[{"source":"PROSITE-ProRule","id":"PRU00433","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 6 |
| Details | Binding site: {"description":"covalent","evidences":[{"source":"PROSITE-ProRule","id":"PRU00433","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 4 |
| Details | Binding site: {"description":"axial binding residue","evidences":[{"source":"PROSITE-ProRule","id":"PRU00433","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 680 |
| Details | Transmembrane: {"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI12 |
| Number of Residues | 94 |
| Details | Topological domain: {"description":"Periplasmic","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI13 |
| Number of Residues | 134 |
| Details | Topological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI14 |
| Number of Residues | 198 |
| Details | Topological domain: {"description":"Extracellular","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI15 |
| Number of Residues | 5 |
| Details | Binding site: {"description":"axial binding residue","evidences":[{"evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI16 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI17 |
| Number of Residues | 2 |
| Details | Cross-link: {"description":"1'-histidyl-3'-tyrosine (His-Tyr)","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI18 |
| Number of Residues | 236 |
| Details | Region: {"description":"Cytochrome c oxidase subunit II"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI19 |
| Number of Residues | 2 |
| Details | Binding site: {"description":"covalent","evidences":[{"evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI20 |
| Number of Residues | 1 |
| Details | Lipidation: {"description":"S-diacylglycerol cysteine","evidences":[{"source":"PROSITE-ProRule","id":"PRU00303","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
