2AVF
Crystal Structure of C-terminal Desundecapeptide Nitrite Reductase from Achromobacter cycloclastes
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 |
| D | 0005507 | molecular_function | copper ion binding |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0019333 | biological_process | denitrification pathway |
| D | 0042128 | biological_process | nitrate assimilation |
| D | 0042597 | cellular_component | periplasmic space |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0050421 | molecular_function | nitrite reductase (NO-forming) activity |
| E | 0005507 | molecular_function | copper ion binding |
| E | 0016491 | molecular_function | oxidoreductase activity |
| E | 0019333 | biological_process | denitrification pathway |
| E | 0042128 | biological_process | nitrate assimilation |
| E | 0042597 | cellular_component | periplasmic space |
| E | 0046872 | molecular_function | metal ion binding |
| E | 0050421 | molecular_function | nitrite reductase (NO-forming) activity |
| F | 0005507 | molecular_function | copper ion binding |
| F | 0016491 | molecular_function | oxidoreductase activity |
| F | 0019333 | biological_process | denitrification pathway |
| F | 0042128 | biological_process | nitrate assimilation |
| F | 0042597 | cellular_component | periplasmic space |
| F | 0046872 | molecular_function | metal ion binding |
| F | 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 502 |
| Chain | Residue |
| A | HIS100 |
| A | HIS135 |
| B | HIS306 |
| B | CL601 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CU B 502 |
| Chain | Residue |
| B | HIS100 |
| B | HIS135 |
| B | CL602 |
| C | HIS306 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CU C 502 |
| Chain | Residue |
| C | HIS100 |
| C | HIS135 |
| C | CL603 |
| A | HIS306 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CU D 502 |
| Chain | Residue |
| D | HIS100 |
| D | HIS135 |
| D | CL604 |
| E | HIS306 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CU E 502 |
| Chain | Residue |
| E | HIS100 |
| E | HIS135 |
| F | HIS306 |
| F | CL605 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CU F 502 |
| Chain | Residue |
| D | HIS306 |
| F | HIS100 |
| F | HIS135 |
| F | CL606 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CU A 501 |
| Chain | Residue |
| A | HIS95 |
| A | CYS136 |
| A | HIS145 |
| A | MET150 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CU B 501 |
| Chain | Residue |
| B | HIS95 |
| B | CYS136 |
| B | HIS145 |
| B | MET150 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CU C 501 |
| Chain | Residue |
| C | HIS95 |
| C | CYS136 |
| C | HIS145 |
| C | MET150 |
| site_id | BC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CU D 501 |
| Chain | Residue |
| D | HIS95 |
| D | CYS136 |
| D | HIS145 |
| D | MET150 |
| site_id | BC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CU E 501 |
| Chain | Residue |
| E | HIS95 |
| E | CYS136 |
| E | HIS145 |
| E | MET150 |
| site_id | BC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CU F 501 |
| Chain | Residue |
| F | HIS95 |
| F | CYS136 |
| F | HIS145 |
| F | MET150 |
| site_id | BC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE CL B 601 |
| Chain | Residue |
| A | ASP98 |
| A | HIS100 |
| A | HIS135 |
| A | CU502 |
| B | HIS255 |
| B | ILE257 |
| B | HIS306 |
| site_id | BC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CL B 602 |
| Chain | Residue |
| B | HIS100 |
| B | HIS135 |
| B | CU502 |
| C | HIS255 |
| C | ILE257 |
| site_id | BC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE CL C 603 |
| Chain | Residue |
| A | HIS255 |
| A | ILE257 |
| A | HIS306 |
| C | ASP98 |
| C | HIS100 |
| C | HIS135 |
| C | CU502 |
| site_id | BC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CL D 604 |
| Chain | Residue |
| D | HIS100 |
| D | HIS135 |
| D | CU502 |
| E | HIS255 |
| E | HIS306 |
| site_id | BC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CL F 605 |
| Chain | Residue |
| E | HIS100 |
| E | HIS135 |
| E | CU502 |
| F | HIS255 |
| F | ILE257 |
| F | HIS306 |
| site_id | BC9 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE CL F 606 |
| Chain | Residue |
| D | HIS255 |
| D | ILE257 |
| D | HIS306 |
| F | ASP98 |
| F | HIS100 |
| F | HIS135 |
| F | CU502 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 24 |
| Details | Binding site: {"description":"type 1 copper site"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 18 |
| Details | Binding site: {"description":"type 2 copper site"} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1nid |
| Chain | Residue | Details |
| F | PHE64 | |
| F | GLY66 |
| site_id | CSA10 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1nid |
| Chain | Residue | Details |
| D | ASP98 | |
| D | HIS255 |
| site_id | CSA11 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1nid |
| Chain | Residue | Details |
| E | ASP98 | |
| E | HIS255 |
| site_id | CSA12 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1nid |
| Chain | Residue | Details |
| F | ASP98 | |
| F | HIS255 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1nid |
| Chain | Residue | Details |
| A | PHE64 | |
| A | GLY66 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1nid |
| Chain | Residue | Details |
| B | PHE64 | |
| B | GLY66 |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1nid |
| Chain | Residue | Details |
| C | PHE64 | |
| C | GLY66 |
| site_id | CSA5 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1nid |
| Chain | Residue | Details |
| D | PHE64 | |
| D | GLY66 |
| site_id | CSA6 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1nid |
| Chain | Residue | Details |
| E | PHE64 | |
| E | GLY66 |
| site_id | CSA7 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1nid |
| Chain | Residue | Details |
| A | ASP98 | |
| A | HIS255 |
| site_id | CSA8 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1nid |
| Chain | Residue | Details |
| B | ASP98 | |
| B | HIS255 |
| site_id | CSA9 |
| 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 |
| site_id | MCSA4 |
| Number of Residues | 11 |
| Details | M-CSA 4 |
| Chain | Residue | Details |
| D | HIS95 | metal ligand |
| D | THR280 | electrostatic stabiliser, modifies pKa |
| D | HIS306 | metal ligand |
| D | ASP98 | activator, hydrogen bond acceptor, proton acceptor, proton donor |
| D | HIS100 | metal ligand |
| D | HIS135 | metal ligand, single electron acceptor, single electron donor, single electron relay |
| D | CYS136 | metal ligand, single electron acceptor, single electron donor, single electron relay |
| D | HIS145 | metal ligand |
| D | MET150 | metal ligand |
| D | HIS255 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| D | GLU279 | electrostatic stabiliser, modifies pKa |
| site_id | MCSA5 |
| Number of Residues | 11 |
| Details | M-CSA 4 |
| Chain | Residue | Details |
| E | HIS95 | metal ligand |
| E | THR280 | electrostatic stabiliser, modifies pKa |
| E | HIS306 | metal ligand |
| E | ASP98 | activator, hydrogen bond acceptor, proton acceptor, proton donor |
| E | HIS100 | metal ligand |
| E | HIS135 | metal ligand, single electron acceptor, single electron donor, single electron relay |
| E | CYS136 | metal ligand, single electron acceptor, single electron donor, single electron relay |
| E | HIS145 | metal ligand |
| E | MET150 | metal ligand |
| E | HIS255 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| E | GLU279 | electrostatic stabiliser, modifies pKa |
| site_id | MCSA6 |
| Number of Residues | 11 |
| Details | M-CSA 4 |
| Chain | Residue | Details |
| F | HIS95 | metal ligand |
| F | THR280 | electrostatic stabiliser, modifies pKa |
| F | HIS306 | metal ligand |
| F | ASP98 | activator, hydrogen bond acceptor, proton acceptor, proton donor |
| F | HIS100 | metal ligand |
| F | HIS135 | metal ligand, single electron acceptor, single electron donor, single electron relay |
| F | CYS136 | metal ligand, single electron acceptor, single electron donor, single electron relay |
| F | HIS145 | metal ligand |
| F | MET150 | metal ligand |
| F | HIS255 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| F | GLU279 | electrostatic stabiliser, modifies pKa |
