1RZP
Crystal Structure of C-Terminal Despentapeptide Nitrite Reductase from Achromobacter Cycloclastes at pH6.2
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 | HOH3003 |
| 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 | 4 |
| Details | BINDING SITE FOR RESIDUE CU B 502 |
| Chain | Residue |
| B | HIS100 |
| B | HIS135 |
| B | HOH2003 |
| 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 | HOH3002 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 C 3001 |
| Chain | Residue |
| C | PHE24 |
| C | LYS174 |
| C | TYR176 |
| C | THR234 |
| C | HOH3030 |
| C | HOH3168 |
| 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 | HOH3051 |
| A | HOH3116 |
| A | HOH3205 |
| site_id | AC9 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE MES C 2001 |
| Chain | Residue |
| C | HIS28 |
| C | GLN30 |
| C | ASP173 |
| C | LYS174 |
| C | ILE175 |
| C | HOH3052 |
| C | HOH3170 |
| C | HOH3179 |
| C | HOH3192 |
| C | HOH3231 |
| site_id | BC1 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE MES B 2002 |
| Chain | Residue |
| B | HIS28 |
| B | GLN30 |
| B | ASP173 |
| B | LYS174 |
| B | ILE175 |
| B | HOH2018 |
| B | HOH2131 |
| B | HOH2135 |
| B | HOH2225 |
| B | HOH2249 |
| C | HOH3183 |
| C | HOH3200 |
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 |
