1RZQ
Crystal Structure of C-Terminal Despentapeptide Nitrite Reductase from Achromobacter Cycloclastes at pH5.0
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005507 | molecular_function | copper ion binding |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0019333 | biological_process | denitrification pathway |
| A | 0042128 | biological_process | nitrate assimilation |
| A | 0042597 | cellular_component | periplasmic space |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0050421 | molecular_function | nitrite reductase (NO-forming) activity |
| B | 0005507 | molecular_function | copper ion binding |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0019333 | biological_process | denitrification pathway |
| B | 0042128 | biological_process | nitrate assimilation |
| B | 0042597 | cellular_component | periplasmic space |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0050421 | molecular_function | nitrite reductase (NO-forming) activity |
| C | 0005507 | molecular_function | copper ion binding |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0019333 | biological_process | denitrification pathway |
| C | 0042128 | biological_process | nitrate assimilation |
| C | 0042597 | cellular_component | periplasmic space |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0050421 | molecular_function | nitrite reductase (NO-forming) activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CU A 501 |
| Chain | Residue |
| A | HIS95 |
| A | CYS136 |
| A | HIS145 |
| A | MET150 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CU A 502 |
| Chain | Residue |
| A | ASP98 |
| A | HIS100 |
| A | HIS135 |
| A | HOH3006 |
| B | HIS306 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CU B 501 |
| Chain | Residue |
| B | HIS95 |
| B | CYS136 |
| B | HIS145 |
| B | MET150 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CU B 502 |
| Chain | Residue |
| B | ASP98 |
| B | HIS100 |
| B | HIS135 |
| B | HOH3005 |
| C | HIS306 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CU C 501 |
| Chain | Residue |
| C | HIS95 |
| C | CYS136 |
| C | HIS145 |
| C | MET150 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CU C 502 |
| Chain | Residue |
| A | HIS306 |
| C | ASP98 |
| C | HIS100 |
| C | HIS135 |
| C | HOH3004 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 B 3001 |
| Chain | Residue |
| B | THR34 |
| B | GLY35 |
| B | ARG37 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 A 3002 |
| Chain | Residue |
| A | PHE24 |
| A | LYS174 |
| A | TYR176 |
| A | THR234 |
| A | HOH3035 |
| A | HOH3143 |
| A | HOH3263 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 C 3003 |
| Chain | Residue |
| C | PHE24 |
| C | LYS174 |
| C | TYR176 |
| C | THR234 |
| C | HOH3020 |
| C | HOH3190 |
| site_id | BC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 B 3004 |
| Chain | Residue |
| B | THR228 |
| B | GLY229 |
| B | HIS319 |
| B | LYS321 |
| site_id | BC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 A 3005 |
| Chain | Residue |
| A | THR228 |
| A | ASP230 |
| A | HIS231 |
| site_id | BC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE ACY A 2001 |
| Chain | Residue |
| A | GLY140 |
| A | MET141 |
| A | VAL142 |
| A | PRO143 |
| A | TRP144 |
| A | TYR203 |
| A | MET210 |
| B | GLU313 |
| site_id | BC4 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE ACY A 2002 |
| Chain | Residue |
| A | THR216 |
| A | HIS217 |
| A | VAL224 |
| A | GLU313 |
| A | LEU314 |
| A | HOH3223 |
| A | HOH3255 |
| C | ARG211 |
| site_id | BC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE ACY C 2003 |
| Chain | Residue |
| C | GLY229 |
| C | HIS319 |
| C | LYS321 |
| site_id | BC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE ACY A 2004 |
| Chain | Residue |
| A | GLY229 |
| A | HIS319 |
| A | LYS321 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 12 |
| Details | BINDING: type 1 copper site |
| Chain | Residue | Details |
| A | HIS95 | |
| C | CYS136 | |
| C | HIS145 | |
| C | MET150 | |
| A | CYS136 | |
| A | HIS145 | |
| A | MET150 | |
| B | HIS95 | |
| B | CYS136 | |
| B | HIS145 | |
| B | MET150 | |
| C | HIS95 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 9 |
| Details | BINDING: type 2 copper site |
| Chain | Residue | Details |
| A | HIS100 | |
| A | HIS135 | |
| A | HIS306 | |
| B | HIS100 | |
| B | HIS135 | |
| B | HIS306 | |
| C | HIS100 | |
| C | HIS135 | |
| C | HIS306 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1nid |
| Chain | Residue | Details |
| A | PHE64 | |
| A | GLY66 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1nid |
| Chain | Residue | Details |
| B | PHE64 | |
| B | GLY66 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1nid |
| Chain | Residue | Details |
| C | PHE64 | |
| C | GLY66 |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1nid |
| Chain | Residue | Details |
| A | ASP98 | |
| A | HIS255 |
| site_id | CSA5 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1nid |
| Chain | Residue | Details |
| B | ASP98 | |
| B | HIS255 |
| site_id | CSA6 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1nid |
| Chain | Residue | Details |
| C | ASP98 | |
| C | HIS255 |
| site_id | MCSA1 |
| Number of Residues | 11 |
| Details | M-CSA 4 |
| Chain | Residue | Details |
| A | HIS95 | metal ligand |
| A | THR280 | electrostatic stabiliser, modifies pKa |
| A | HIS306 | metal ligand |
| A | ASP98 | activator, hydrogen bond acceptor, proton acceptor, proton donor |
| A | HIS100 | metal ligand |
| A | HIS135 | metal ligand, single electron acceptor, single electron donor, single electron relay |
| A | CYS136 | metal ligand, single electron acceptor, single electron donor, single electron relay |
| A | HIS145 | metal ligand |
| A | MET150 | metal ligand |
| A | HIS255 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| A | GLU279 | electrostatic stabiliser, modifies pKa |
| site_id | MCSA2 |
| Number of Residues | 11 |
| Details | M-CSA 4 |
| Chain | Residue | Details |
| B | HIS95 | metal ligand |
| B | THR280 | electrostatic stabiliser, modifies pKa |
| B | HIS306 | metal ligand |
| B | ASP98 | activator, hydrogen bond acceptor, proton acceptor, proton donor |
| B | HIS100 | metal ligand |
| B | HIS135 | metal ligand, single electron acceptor, single electron donor, single electron relay |
| B | CYS136 | metal ligand, single electron acceptor, single electron donor, single electron relay |
| B | HIS145 | metal ligand |
| B | MET150 | metal ligand |
| B | HIS255 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| B | GLU279 | electrostatic stabiliser, modifies pKa |
| site_id | MCSA3 |
| Number of Residues | 11 |
| Details | M-CSA 4 |
| Chain | Residue | Details |
| C | HIS95 | metal ligand |
| C | THR280 | electrostatic stabiliser, modifies pKa |
| C | HIS306 | metal ligand |
| C | ASP98 | activator, hydrogen bond acceptor, proton acceptor, proton donor |
| C | HIS100 | metal ligand |
| C | HIS135 | metal ligand, single electron acceptor, single electron donor, single electron relay |
| C | CYS136 | metal ligand, single electron acceptor, single electron donor, single electron relay |
| C | HIS145 | metal ligand |
| C | MET150 | metal ligand |
| C | HIS255 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| C | GLU279 | electrostatic stabiliser, modifies pKa |
