Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004129 | molecular_function | cytochrome-c oxidase activity |
A | 0005886 | cellular_component | plasma membrane |
A | 0006119 | biological_process | oxidative phosphorylation |
A | 0009060 | biological_process | aerobic respiration |
A | 0015990 | biological_process | electron transport coupled proton transport |
A | 0016020 | cellular_component | membrane |
A | 0020037 | molecular_function | heme binding |
A | 0022904 | biological_process | respiratory electron transport chain |
A | 0045277 | cellular_component | respiratory chain complex IV |
A | 0046872 | molecular_function | metal ion binding |
A | 0070469 | cellular_component | respirasome |
A | 1902600 | biological_process | proton transmembrane transport |
B | 0004129 | molecular_function | cytochrome-c oxidase activity |
B | 0005507 | molecular_function | copper ion binding |
B | 0016020 | cellular_component | membrane |
B | 0016491 | molecular_function | oxidoreductase activity |
B | 0022900 | biological_process | electron transport chain |
C | 0002250 | biological_process | adaptive immune response |
C | 0003823 | molecular_function | antigen binding |
C | 0016064 | biological_process | immunoglobulin mediated immune response |
C | 0019814 | cellular_component | immunoglobulin complex |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CU B 270 |
Chain | Residue |
B | CYS216 |
B | GLU218 |
B | CYS220 |
B | HIS224 |
B | CU271 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CU B 271 |
Chain | Residue |
B | HIS181 |
B | CYS216 |
B | CYS220 |
B | MET227 |
B | CU270 |
site_id | AC3 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CU A 559 |
Chain | Residue |
A | HIS276 |
A | HIS325 |
A | HIS326 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG A 560 |
Chain | Residue |
A | HIS403 |
A | ASP404 |
A | HOH574 |
B | SER217 |
B | GLU218 |
site_id | AC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CA A 561 |
Chain | Residue |
A | GLU56 |
A | HIS59 |
A | GLY61 |
A | GLN63 |
A | ASP477 |
site_id | AC6 |
Number of Residues | 21 |
Details | BINDING SITE FOR RESIDUE HEA A 562 |
Chain | Residue |
A | THR50 |
A | ARG54 |
A | TRP87 |
A | ILE91 |
A | HIS94 |
A | MET98 |
A | MET99 |
A | VAL103 |
A | GLY163 |
A | TRP164 |
A | TYR406 |
A | HIS413 |
A | MET416 |
A | SER417 |
A | PHE460 |
A | ARG473 |
A | ARG474 |
A | TYR475 |
A | SER496 |
A | PHE503 |
A | HOH575 |
site_id | AC7 |
Number of Residues | 25 |
Details | BINDING SITE FOR RESIDUE HEA A 563 |
Chain | Residue |
A | TRP164 |
A | TRP272 |
A | VAL279 |
A | TYR280 |
A | HIS325 |
A | HIS326 |
A | THR344 |
A | ILE347 |
A | ALA348 |
A | THR351 |
A | GLY352 |
A | GLY387 |
A | GLY390 |
A | LEU393 |
A | SER394 |
A | ASP399 |
A | HIS403 |
A | VAL408 |
A | HIS411 |
A | PHE412 |
A | VAL415 |
A | MET416 |
A | ARG473 |
A | HOH571 |
A | HOH572 |
site_id | AC8 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE LDA B 272 |
Chain | Residue |
A | PHE465 |
A | ARG468 |
A | LDA569 |
B | ASN19 |
site_id | AC9 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE LDA B 273 |
site_id | BC1 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE LDA A 564 |
site_id | BC2 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE LDA A 565 |
Chain | Residue |
A | TRP363 |
B | ASN74 |
B | TRP81 |
site_id | BC3 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE LDA A 566 |
Chain | Residue |
A | LEU511 |
A | ILE33 |
A | SER436 |
site_id | BC4 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE LDA A 568 |
Chain | Residue |
A | TRP443 |
A | GLY505 |
A | ILE506 |
site_id | BC5 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE LDA B 274 |
Chain | Residue |
B | VAL90 |
B | ALA94 |
B | PRO98 |
site_id | BC6 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE LDA A 569 |
Chain | Residue |
A | PHE461 |
B | LDA272 |
site_id | CA |
Number of Residues | 4 |
Details | NON REDOX ACTIVE CA BINDING SITE. |
Chain | Residue |
A | GLU56 |
A | HIS59 |
A | GLY61 |
A | GLN63 |
site_id | CUA |
Number of Residues | 6 |
Details | CU A BINDING SITE. |
Chain | Residue |
B | HIS181 |
B | CYS216 |
B | GLU218 |
B | CYS220 |
B | HIS224 |
B | MET227 |
site_id | CUB |
Number of Residues | 3 |
Details | CU B BINDING SITE. |
Chain | Residue |
A | HIS276 |
A | HIS325 |
A | HIS326 |
site_id | HM3 |
Number of Residues | 1 |
Details | AXIAL HEME A3 LIGAND. |
site_id | HMA |
Number of Residues | 2 |
Details | AXIAL HEME A LIGANDS. |
Chain | Residue |
A | HIS94 |
A | HIS413 |
site_id | MM |
Number of Residues | 3 |
Details | NON REDOX ACTIVE MN/MG BINDING SITE. |
Chain | Residue |
A | HIS403 |
A | ASP404 |
B | GLU218 |
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. WFFGHPeVyiiilpgfgiishvistfakkpifgylpmvlamaaigilgfvvwa..HH |
Chain | Residue | Details |
A | TRP272-HIS326 | |
site_id | PS00078 |
Number of Residues | 49 |
Details | COX2 CO II and nitrous oxide reductase dinuclear copper centers signature. ViHawtipafavkqdavpgriaqlwfsvdqegvyfgq......CselCginHayM |
Chain | Residue | Details |
B | VAL179-MET227 | |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 170 |
Details | TOPO_DOM: Periplasmic |
Chain | Residue | Details |
B | GLN1-PRO26 | |
B | MET106-ALA251 | |
A | MET207-VAL217 | |
A | LYS300-PHE303 | |
A | GLY365-PHE369 | |
A | ARG438-TYR440 | |
A | LYS515-HIS558 | |
site_id | SWS_FT_FI2 |
Number of Residues | 62 |
Details | TRANSMEM: Helical |
Chain | Residue | Details |
B | LEU27-ARG59 | |
B | THR75-GLU105 | |
site_id | SWS_FT_FI3 |
Number of Residues | 14 |
Details | TOPO_DOM: Cytoplasmic |
Chain | Residue | Details |
B | PHE60-ASN74 | |
A | PRO152-GLY176 | |
A | GLY252-GLY262 | |
A | MET332 | |
A | ALA396-ASP404 | |
A | GLY470-TYR478 | |
site_id | SWS_FT_FI4 |
Number of Residues | 6 |
Details | BINDING: |
Chain | Residue | Details |
B | HIS181 | |
B | CYS216 | |
B | GLU218 | |
B | CYS220 | |
B | HIS224 | |
B | MET227 | |
site_id | SWS_FT_FI6 |
Number of Residues | 29 |
Details | TRANSMEM: Helical; Name=IV |
Chain | Residue | Details |
A | TYR177-ASN206 | |
site_id | SWS_FT_FI7 |
Number of Residues | 33 |
Details | TRANSMEM: Helical; Name=V |
Chain | Residue | Details |
A | PRO218-PHE251 | |
site_id | SWS_FT_FI8 |
Number of Residues | 36 |
Details | TRANSMEM: Helical; Name=VI |
Chain | Residue | Details |
A | ASP263-LYS299 | |
site_id | SWS_FT_FI9 |
Number of Residues | 27 |
Details | TRANSMEM: Helical; Name=VII |
Chain | Residue | Details |
A | GLY304-GLY331 | |
site_id | SWS_FT_FI10 |
Number of Residues | 31 |
Details | TRANSMEM: Helical; Name=VIII |
Chain | Residue | Details |
A | SER333-GLY364 | |
site_id | SWS_FT_FI11 |
Number of Residues | 25 |
Details | TRANSMEM: Helical; Name=IX |
Chain | Residue | Details |
A | LYS370-GLN395 | |
site_id | SWS_FT_FI12 |
Number of Residues | 32 |
Details | TRANSMEM: Helical; Name=X |
Chain | Residue | Details |
A | THR405-GLY437 | |
site_id | SWS_FT_FI13 |
Number of Residues | 28 |
Details | TRANSMEM: Helical; Name=XI |
Chain | Residue | Details |
A | PRO441-GLN469 | |
site_id | SWS_FT_FI14 |
Number of Residues | 35 |
Details | TRANSMEM: Helical; Name=XII |
Chain | Residue | Details |
A | PRO479-GLY514 | |
site_id | SWS_FT_FI15 |
Number of Residues | 3 |
Details | BINDING: axial binding residue |
Chain | Residue | Details |
A | HIS94 | |
A | HIS411 | |
A | HIS413 | |
site_id | SWS_FT_FI16 |
Number of Residues | 4 |
Details | BINDING: |
Chain | Residue | Details |
A | HIS276 | |
A | TYR280 | |
A | HIS325 | |
A | HIS326 | |
site_id | SWS_FT_FI17 |
Number of Residues | 2 |
Details | CROSSLNK: 1'-histidyl-3'-tyrosine (His-Tyr) |
Chain | Residue | Details |
A | HIS276 | |
A | TYR280 | |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 2 |
Details | a catalytic site defined by CSA, PubMed 9788998 |
Chain | Residue | Details |
A | GLU278 | |
A | LYS354 | |