1QNI
Crystal Structure of Nitrous Oxide Reductase from Pseudomonas nautica, at 2.4A Resolution
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004129 | molecular_function | cytochrome-c oxidase activity |
| A | 0005507 | molecular_function | copper ion binding |
| A | 0005509 | molecular_function | calcium ion binding |
| A | 0016020 | cellular_component | membrane |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0042597 | cellular_component | periplasmic space |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0050304 | molecular_function | nitrous-oxide reductase activity |
| A | 1902600 | biological_process | proton transmembrane transport |
| B | 0004129 | molecular_function | cytochrome-c oxidase activity |
| B | 0005507 | molecular_function | copper ion binding |
| B | 0005509 | molecular_function | calcium ion binding |
| B | 0016020 | cellular_component | membrane |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0042597 | cellular_component | periplasmic space |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0050304 | molecular_function | nitrous-oxide reductase activity |
| B | 1902600 | biological_process | proton transmembrane transport |
| C | 0004129 | molecular_function | cytochrome-c oxidase activity |
| C | 0005507 | molecular_function | copper ion binding |
| C | 0005509 | molecular_function | calcium ion binding |
| C | 0016020 | cellular_component | membrane |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0042597 | cellular_component | periplasmic space |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0050304 | molecular_function | nitrous-oxide reductase activity |
| C | 1902600 | biological_process | proton transmembrane transport |
| D | 0004129 | molecular_function | cytochrome-c oxidase activity |
| D | 0005507 | molecular_function | copper ion binding |
| D | 0005509 | molecular_function | calcium ion binding |
| D | 0016020 | cellular_component | membrane |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0042597 | cellular_component | periplasmic space |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0050304 | molecular_function | nitrous-oxide reductase activity |
| D | 1902600 | biological_process | proton transmembrane transport |
| E | 0004129 | molecular_function | cytochrome-c oxidase activity |
| E | 0005507 | molecular_function | copper ion binding |
| E | 0005509 | molecular_function | calcium ion binding |
| E | 0016020 | cellular_component | membrane |
| E | 0016491 | molecular_function | oxidoreductase activity |
| E | 0042597 | cellular_component | periplasmic space |
| E | 0046872 | molecular_function | metal ion binding |
| E | 0050304 | molecular_function | nitrous-oxide reductase activity |
| E | 1902600 | biological_process | proton transmembrane transport |
| F | 0004129 | molecular_function | cytochrome-c oxidase activity |
| F | 0005507 | molecular_function | copper ion binding |
| F | 0005509 | molecular_function | calcium ion binding |
| F | 0016020 | cellular_component | membrane |
| F | 0016491 | molecular_function | oxidoreductase activity |
| F | 0042597 | cellular_component | periplasmic space |
| F | 0046872 | molecular_function | metal ion binding |
| F | 0050304 | molecular_function | nitrous-oxide reductase activity |
| F | 1902600 | biological_process | proton transmembrane transport |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA A 901 |
| Chain | Residue |
| A | TYR204 |
| A | GLU207 |
| A | THR215 |
| A | ASP221 |
| A | ASN268 |
| A | HOH2172 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CL A 902 |
| Chain | Residue |
| A | ASN273 |
| A | HIS325 |
| A | ARG131 |
| A | GLY271 |
| A | LEU272 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA A 903 |
| Chain | Residue |
| A | LYS397 |
| A | GLU412 |
| A | HOH2235 |
| A | HOH2236 |
| B | HOH2288 |
| B | HOH2309 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA B 901 |
| Chain | Residue |
| B | TYR204 |
| B | GLU207 |
| B | THR215 |
| B | ASP221 |
| B | ASN268 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CL B 902 |
| Chain | Residue |
| B | ARG131 |
| B | ASN189 |
| B | LEU272 |
| B | ASN273 |
| B | HIS325 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA B 903 |
| Chain | Residue |
| A | HOH2309 |
| B | LYS397 |
| B | GLU412 |
| B | HOH2200 |
| B | HOH2209 |
| B | HOH2210 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA C 901 |
| Chain | Residue |
| C | TYR204 |
| C | GLU207 |
| C | THR215 |
| C | ASP221 |
| C | ASN268 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CL C 902 |
| Chain | Residue |
| C | ARG131 |
| C | ASN189 |
| C | LEU272 |
| C | ASN273 |
| C | HIS325 |
| site_id | AC9 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CA C 903 |
| Chain | Residue |
| C | LYS397 |
| C | GLU412 |
| D | HOH2100 |
| site_id | BC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA D 901 |
| Chain | Residue |
| D | TYR204 |
| D | GLU207 |
| D | THR215 |
| D | ASP221 |
| D | ASN268 |
| site_id | BC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CL D 902 |
| Chain | Residue |
| D | ARG131 |
| D | GLY271 |
| D | LEU272 |
| D | ASN273 |
| D | HIS325 |
| site_id | BC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA D 903 |
| Chain | Residue |
| C | ASP523 |
| C | HOH2089 |
| D | LYS397 |
| D | GLU412 |
| D | HOH2068 |
| site_id | BC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA E 901 |
| Chain | Residue |
| E | TYR204 |
| E | GLU207 |
| E | THR215 |
| E | ASP221 |
| E | ASN268 |
| site_id | BC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CL E 902 |
| Chain | Residue |
| E | ARG131 |
| E | GLY271 |
| E | LEU272 |
| E | ASN273 |
| E | HIS325 |
| site_id | BC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA E 903 |
| Chain | Residue |
| E | LYS397 |
| E | GLU412 |
| E | HOH2172 |
| E | HOH2181 |
| F | HOH2200 |
| site_id | BC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA F 901 |
| Chain | Residue |
| F | TYR204 |
| F | GLU207 |
| F | THR215 |
| F | ASP221 |
| F | ASN268 |
| site_id | BC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CL F 902 |
| Chain | Residue |
| F | ARG131 |
| F | ASN189 |
| F | GLY271 |
| F | LEU272 |
| F | ASN273 |
| F | HIS325 |
| site_id | BC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CA F 903 |
| Chain | Residue |
| E | HOH2214 |
| F | LYS397 |
| F | GLU412 |
| F | HOH2133 |
| site_id | CC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CUA A 701 |
| Chain | Residue |
| A | HIS526 |
| A | CYS561 |
| A | TRP563 |
| A | CYS565 |
| A | HIS569 |
| A | MET572 |
| site_id | CC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE CUZ A 801 |
| Chain | Residue |
| A | HIS128 |
| A | HIS270 |
| A | HIS325 |
| A | HIS376 |
| A | HIS437 |
| A | HOH2252 |
| A | HIS79 |
| A | HIS80 |
| site_id | CC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CUA B 701 |
| Chain | Residue |
| B | HIS526 |
| B | CYS561 |
| B | TRP563 |
| B | CYS565 |
| B | HIS569 |
| B | MET572 |
| site_id | CC4 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE CUZ B 801 |
| Chain | Residue |
| B | HIS79 |
| B | HIS80 |
| B | HIS128 |
| B | HIS270 |
| B | HIS325 |
| B | HIS376 |
| B | HIS437 |
| B | HOH2201 |
| site_id | CC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CUA C 701 |
| Chain | Residue |
| C | HIS526 |
| C | CYS561 |
| C | TRP563 |
| C | CYS565 |
| C | HIS569 |
| C | MET572 |
| site_id | CC6 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE CUZ C 801 |
| Chain | Residue |
| C | HIS79 |
| C | HIS80 |
| C | HIS128 |
| C | HIS270 |
| C | HIS325 |
| C | HIS376 |
| C | HIS437 |
| C | HOH2060 |
| site_id | CC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CUA D 701 |
| Chain | Residue |
| D | HIS526 |
| D | CYS561 |
| D | TRP563 |
| D | CYS565 |
| D | HIS569 |
| D | MET572 |
| site_id | CC8 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE CUZ D 801 |
| Chain | Residue |
| C | HOH2036 |
| D | HIS79 |
| D | HIS80 |
| D | HIS128 |
| D | HIS270 |
| D | HIS325 |
| D | HIS376 |
| D | HIS437 |
| D | HOH2064 |
| site_id | CC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CUA E 701 |
| Chain | Residue |
| E | HIS526 |
| E | CYS561 |
| E | TRP563 |
| E | CYS565 |
| E | HIS569 |
| E | MET572 |
| site_id | DC1 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE CUZ E 801 |
| Chain | Residue |
| E | HIS79 |
| E | HIS80 |
| E | HIS128 |
| E | HIS270 |
| E | HIS325 |
| E | HIS376 |
| E | HIS437 |
| E | HOH2171 |
| site_id | DC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CUA F 701 |
| Chain | Residue |
| F | HIS526 |
| F | CYS561 |
| F | TRP563 |
| F | CYS565 |
| F | HIS569 |
| F | MET572 |
| site_id | DC3 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE CUZ F 801 |
| Chain | Residue |
| F | HIS79 |
| F | HIS80 |
| F | HIS128 |
| F | ASN189 |
| F | HIS270 |
| F | HIS325 |
| F | HIS376 |
| F | HIS437 |
| F | HOH2042 |
| F | HOH2094 |
| F | HOH2144 |
Functional Information from PROSITE/UniProt
| site_id | PS00078 |
| Number of Residues | 49 |
| Details | COX2 CO II and nitrous oxide reductase dinuclear copper centers signature. VtHgfcmvnhgvsmeispqqtasvtftagkpgvywyy......CnwfChalHmeM |
| Chain | Residue | Details |
| A | VAL524-MET572 |
