5GUW
Complex of Cytochrome cd1 Nitrite Reductase and Nitric Oxide Reductase in Denitrification of Pseudomonas aeruginosa
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0009055 | molecular_function | electron transfer activity |
| A | 0020037 | molecular_function | heme binding |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0004129 | molecular_function | cytochrome-c oxidase activity |
| B | 0005886 | cellular_component | plasma membrane |
| B | 0009060 | biological_process | aerobic respiration |
| B | 0015990 | biological_process | electron transport coupled proton transport |
| B | 0016020 | cellular_component | membrane |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016966 | molecular_function | nitric oxide reductase activity |
| B | 0019333 | biological_process | denitrification pathway |
| B | 0020037 | molecular_function | heme binding |
| B | 0022904 | biological_process | respiratory electron transport chain |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0005886 | cellular_component | plasma membrane |
| C | 0009055 | molecular_function | electron transfer activity |
| C | 0020037 | molecular_function | heme binding |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0004129 | molecular_function | cytochrome-c oxidase activity |
| D | 0005886 | cellular_component | plasma membrane |
| D | 0009060 | biological_process | aerobic respiration |
| D | 0015990 | biological_process | electron transport coupled proton transport |
| D | 0016020 | cellular_component | membrane |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0016966 | molecular_function | nitric oxide reductase activity |
| D | 0019333 | biological_process | denitrification pathway |
| D | 0020037 | molecular_function | heme binding |
| D | 0022904 | biological_process | respiratory electron transport chain |
| D | 0046872 | molecular_function | metal ion binding |
| M | 0009055 | molecular_function | electron transfer activity |
| M | 0020037 | molecular_function | heme binding |
| N | 0009055 | molecular_function | electron transfer activity |
| N | 0020037 | molecular_function | heme binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 19 |
| Details | binding site for residue HEC A 201 |
| Chain | Residue |
| A | ASN59 |
| A | LEU95 |
| A | TRP98 |
| A | ARG109 |
| A | ARG110 |
| A | ALA111 |
| A | MET112 |
| A | PRO113 |
| A | PHE115 |
| A | LEU125 |
| B | MET427 |
| A | CYS61 |
| A | CYS64 |
| A | HIS65 |
| A | ALA75 |
| A | LEU78 |
| A | VAL81 |
| A | ARG84 |
| A | ARG85 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue CA A 202 |
| Chain | Residue |
| A | GLY71 |
| A | TYR73 |
| B | ARG57 |
| B | GLU135 |
| B | HEM801 |
| B | HEM802 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | binding site for residue 10M A 203 |
| Chain | Residue |
| A | ASN138 |
| A | GLN139 |
| A | PRO142 |
| B | LEU270 |
| B | TRP271 |
| B | TYR336 |
| B | TYR337 |
| site_id | AC4 |
| Number of Residues | 22 |
| Details | binding site for residue HEM B 801 |
| Chain | Residue |
| A | ALA72 |
| A | TYR73 |
| A | PHE74 |
| A | CA202 |
| B | GLN30 |
| B | ILE31 |
| B | GLY34 |
| B | LEU35 |
| B | MET37 |
| B | TYR41 |
| B | PHE53 |
| B | ARG57 |
| B | HIS60 |
| B | LEU64 |
| B | GLU135 |
| B | HIS349 |
| B | PHE352 |
| B | TYR353 |
| B | MET397 |
| B | GLU441 |
| B | PHE447 |
| B | HEM802 |
| site_id | AC5 |
| Number of Residues | 24 |
| Details | binding site for residue HEM B 802 |
| Chain | Residue |
| A | TYR73 |
| A | CA202 |
| B | GLU135 |
| B | VAL210 |
| B | GLU211 |
| B | HIS258 |
| B | HIS259 |
| B | SER277 |
| B | GLU280 |
| B | ALA322 |
| B | GLY326 |
| B | PHE327 |
| B | HIS329 |
| B | THR330 |
| B | ASN335 |
| B | HIS339 |
| B | THR344 |
| B | HIS347 |
| B | ALA351 |
| B | PHE352 |
| B | ALA355 |
| B | TYR356 |
| B | HEM801 |
| B | O804 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | binding site for residue FE B 803 |
| Chain | Residue |
| B | HIS207 |
| B | GLU211 |
| B | HIS258 |
| B | HIS259 |
| B | O804 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | binding site for residue O B 804 |
| Chain | Residue |
| B | GLU211 |
| B | HIS259 |
| B | HEM802 |
| B | FE803 |
| site_id | AC8 |
| Number of Residues | 19 |
| Details | binding site for residue HEC C 201 |
| Chain | Residue |
| C | ALA111 |
| C | MET112 |
| C | PHE115 |
| C | LEU125 |
| D | PHE53 |
| D | ASN54 |
| D | MET427 |
| C | CYS61 |
| C | CYS64 |
| C | HIS65 |
| C | ALA75 |
| C | LEU78 |
| C | VAL81 |
| C | ARG84 |
| C | ARG85 |
| C | LEU95 |
| C | TRP98 |
| C | ARG109 |
| C | ARG110 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | binding site for residue CA C 202 |
| Chain | Residue |
| C | GLY71 |
| C | TYR73 |
| D | GLU135 |
| D | HEM801 |
| D | HEM802 |
| site_id | AD1 |
| Number of Residues | 9 |
| Details | binding site for residue 10M C 203 |
| Chain | Residue |
| C | ASN138 |
| C | GLN139 |
| C | PRO142 |
| C | HOH301 |
| D | LEU270 |
| D | TRP271 |
| D | TYR336 |
| D | TYR337 |
| D | 10M805 |
| site_id | AD2 |
| Number of Residues | 21 |
| Details | binding site for residue HEM D 801 |
| Chain | Residue |
| C | ALA72 |
| C | TYR73 |
| C | PHE74 |
| C | CA202 |
| D | GLN30 |
| D | ILE31 |
| D | GLY34 |
| D | LEU35 |
| D | MET37 |
| D | TYR41 |
| D | PHE53 |
| D | ARG57 |
| D | HIS60 |
| D | LEU64 |
| D | GLU135 |
| D | HIS349 |
| D | PHE352 |
| D | TYR353 |
| D | MET397 |
| D | PHE447 |
| D | HEM802 |
| site_id | AD3 |
| Number of Residues | 26 |
| Details | binding site for residue HEM D 802 |
| Chain | Residue |
| C | CA202 |
| D | GLU135 |
| D | PHE136 |
| D | TRP203 |
| D | VAL210 |
| D | GLU211 |
| D | HIS258 |
| D | HIS259 |
| D | GLU280 |
| D | PHE284 |
| D | ALA322 |
| D | GLY326 |
| D | PHE327 |
| D | HIS329 |
| D | THR330 |
| D | ASN335 |
| D | HIS339 |
| D | GLY340 |
| D | THR344 |
| D | HIS347 |
| D | ALA351 |
| D | PHE352 |
| D | ALA355 |
| D | TYR356 |
| D | HEM801 |
| D | O804 |
| site_id | AD4 |
| Number of Residues | 5 |
| Details | binding site for residue FE D 803 |
| Chain | Residue |
| D | HIS207 |
| D | GLU211 |
| D | HIS258 |
| D | HIS259 |
| D | O804 |
| site_id | AD5 |
| Number of Residues | 4 |
| Details | binding site for residue O D 804 |
| Chain | Residue |
| D | GLU211 |
| D | HIS259 |
| D | HEM802 |
| D | FE803 |
| site_id | AD6 |
| Number of Residues | 4 |
| Details | binding site for residue 10M D 805 |
| Chain | Residue |
| C | 10M203 |
| D | MET328 |
| D | MET417 |
| D | ALA419 |
| site_id | AD7 |
| Number of Residues | 20 |
| Details | binding site for residue DHE M 602 |
| Chain | Residue |
| M | ARG156 |
| M | HIS182 |
| M | ILE183 |
| M | ARG185 |
| M | ARG198 |
| M | ARG225 |
| M | SER226 |
| M | TYR245 |
| M | ALA283 |
| M | ALA284 |
| M | ILE285 |
| M | HIS327 |
| M | ARG372 |
| M | PHE425 |
| M | GLN483 |
| M | TRP498 |
| M | GLY531 |
| M | PHE533 |
| N | TYR10 |
| N | ALA13 |
| site_id | AD8 |
| Number of Residues | 3 |
| Details | binding site for residue CL M 603 |
| Chain | Residue |
| M | GLY268 |
| M | MET269 |
| N | SER265 |
| site_id | AD9 |
| Number of Residues | 19 |
| Details | binding site for residue DHE N 602 |
| Chain | Residue |
| M | TYR10 |
| M | ALA13 |
| N | ARG156 |
| N | HIS182 |
| N | ILE183 |
| N | ARG185 |
| N | ARG198 |
| N | ARG225 |
| N | SER226 |
| N | TYR245 |
| N | ALA283 |
| N | ALA284 |
| N | ILE285 |
| N | HIS327 |
| N | ARG372 |
| N | PHE425 |
| N | GLN483 |
| N | GLY531 |
| N | PHE533 |
| site_id | AE1 |
| Number of Residues | 3 |
| Details | binding site for residue CL N 603 |
| Chain | Residue |
| M | SER265 |
| N | GLY268 |
| N | MET269 |
| site_id | AE2 |
| Number of Residues | 21 |
| Details | binding site for Di-peptide HEC M 601 and CYS M 50 |
| Chain | Residue |
| M | ARG46 |
| M | CYS47 |
| M | ALA48 |
| M | GLY49 |
| M | HIS51 |
| M | GLY52 |
| M | GLY57 |
| M | ALA58 |
| M | THR59 |
| M | LYS61 |
| M | LEU63 |
| M | ARG71 |
| M | TYR75 |
| M | LEU79 |
| M | THR84 |
| M | LEU86 |
| M | GLY87 |
| M | MET88 |
| M | PRO89 |
| M | TRP91 |
| M | ILE109 |
| site_id | AE3 |
| Number of Residues | 19 |
| Details | binding site for Di-peptide HEC M 601 and CYS M 47 |
| Chain | Residue |
| M | TYR43 |
| M | ARG46 |
| M | ALA48 |
| M | GLY49 |
| M | CYS50 |
| M | HIS51 |
| M | THR59 |
| M | LYS61 |
| M | LEU63 |
| M | ARG71 |
| M | TYR75 |
| M | LEU79 |
| M | THR84 |
| M | LEU86 |
| M | GLY87 |
| M | MET88 |
| M | PRO89 |
| M | TRP91 |
| M | ILE109 |
| site_id | AE4 |
| Number of Residues | 20 |
| Details | binding site for Di-peptide HEC N 601 and CYS N 50 |
| Chain | Residue |
| M | GLU8 |
| N | ARG46 |
| N | CYS47 |
| N | ALA48 |
| N | GLY49 |
| N | HIS51 |
| N | GLY52 |
| N | GLY57 |
| N | ALA58 |
| N | THR59 |
| N | LEU63 |
| N | ARG71 |
| N | TYR75 |
| N | LEU79 |
| N | THR84 |
| N | LEU86 |
| N | GLY87 |
| N | MET88 |
| N | TRP91 |
| N | ILE109 |
| site_id | AE5 |
| Number of Residues | 18 |
| Details | binding site for Di-peptide HEC N 601 and CYS N 47 |
| Chain | Residue |
| M | GLU8 |
| N | TYR43 |
| N | ARG46 |
| N | ALA48 |
| N | GLY49 |
| N | CYS50 |
| N | HIS51 |
| N | THR59 |
| N | LEU63 |
| N | ARG71 |
| N | TYR75 |
| N | LEU79 |
| N | THR84 |
| N | LEU86 |
| N | GLY87 |
| N | MET88 |
| N | TRP91 |
| N | ILE109 |
Functional Information from PROSITE/UniProt
| site_id | PS00077 |
| Number of Residues | 57 |
| Details | COX1_CUB Heme-copper oxidase catalytic subunit, copper B binding region signature. WWVVHLwVegvwelimgailafvlvkitgvdreviekwlyviiamalisgiigtgHH |
| Chain | Residue | Details |
| B | TRP203-HIS259 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | BINDING: covalent => ECO:0000269|PubMed:9331415, ECO:0007744|PDB:1NIR |
| Chain | Residue | Details |
| M | CYS47 | |
| B | HIS349-PRO369 | |
| B | TRP391-GLN411 | |
| B | ALA434-TYR454 | |
| D | TYR19-LEU39 | |
| D | THR61-PRO81 | |
| D | TRP95-VAL115 | |
| D | ILE142-VAL162 | |
| D | ALA169-PHE189 | |
| D | VAL205-VAL225 | |
| D | VAL243-ILE263 | |
| M | CYS50 | |
| D | LEU270-PHE290 | |
| D | ALA308-MET328 | |
| D | HIS349-PRO369 | |
| D | TRP391-GLN411 | |
| D | ALA434-TYR454 | |
| N | CYS47 | |
| N | CYS50 | |
| B | ALA169-PHE189 | |
| B | VAL205-VAL225 | |
| B | VAL243-ILE263 | |
| B | LEU270-PHE290 | |
| B | ALA308-MET328 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | BINDING: axial binding residue => ECO:0000269|PubMed:9331415, ECO:0007744|PDB:1NIR |
| Chain | Residue | Details |
| M | HIS51 | |
| M | MET88 | |
| N | HIS51 | |
| N | MET88 | |
| D | GLY348 | |
| D | MET350 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 14 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:9331415, ECO:0007744|PDB:1NIR |
| Chain | Residue | Details |
| M | ARG71 | |
| N | ARG225 | |
| N | SER226 | |
| N | TYR245 | |
| N | ARG372 | |
| N | GLN483 | |
| M | THR84 | |
| M | ARG225 | |
| M | SER226 | |
| M | TYR245 | |
| M | ARG372 | |
| M | GLN483 | |
| N | ARG71 | |
| N | THR84 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | BINDING: proximal binding residue => ECO:0000269|PubMed:9331415, ECO:0007744|PDB:1NIR |
| Chain | Residue | Details |
| M | HIS182 | |
| N | HIS182 |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 6 |
| Details | M-CSA 903 |
| Chain | Residue | Details |
| M | CYS47 | covalently attached |
| M | CYS50 | covalently attached |
| M | HIS51 | metal ligand |
| M | MET88 | metal ligand |
| M | HIS327 | electrostatic stabiliser |
| M | HIS369 | electrostatic stabiliser |
| site_id | MCSA2 |
| Number of Residues | 6 |
| Details | M-CSA 903 |
| Chain | Residue | Details |
| N | CYS47 | covalently attached |
| N | CYS50 | covalently attached |
| N | HIS51 | metal ligand |
| N | MET88 | metal ligand |
| N | HIS327 | electrostatic stabiliser |
| N | HIS369 | electrostatic stabiliser |
