6O7Q
Nitrogenase MoFeP mutant S188A from Azotobacter vinelandii in the dithionite reduced state after redox cycling
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005524 | molecular_function | ATP binding |
| A | 0009399 | biological_process | nitrogen fixation |
| A | 0016163 | molecular_function | nitrogenase activity |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016612 | cellular_component | molybdenum-iron nitrogenase complex |
| A | 0018697 | molecular_function | obsolete carbonyl sulfide nitrogenase activity |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0051536 | molecular_function | iron-sulfur cluster binding |
| B | 0005524 | molecular_function | ATP binding |
| B | 0009399 | biological_process | nitrogen fixation |
| B | 0016163 | molecular_function | nitrogenase activity |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016612 | cellular_component | molybdenum-iron nitrogenase complex |
| B | 0018697 | molecular_function | obsolete carbonyl sulfide nitrogenase activity |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0051536 | molecular_function | iron-sulfur cluster binding |
| C | 0005524 | molecular_function | ATP binding |
| C | 0009399 | biological_process | nitrogen fixation |
| C | 0016163 | molecular_function | nitrogenase activity |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0016612 | cellular_component | molybdenum-iron nitrogenase complex |
| C | 0018697 | molecular_function | obsolete carbonyl sulfide nitrogenase activity |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0051536 | molecular_function | iron-sulfur cluster binding |
| D | 0005524 | molecular_function | ATP binding |
| D | 0009399 | biological_process | nitrogen fixation |
| D | 0016163 | molecular_function | nitrogenase activity |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0016612 | cellular_component | molybdenum-iron nitrogenase complex |
| D | 0018697 | molecular_function | obsolete carbonyl sulfide nitrogenase activity |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0051536 | molecular_function | iron-sulfur cluster binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 14 |
| Details | binding site for residue CLF A 501 |
| Chain | Residue |
| A | CYS62 |
| B | SER92 |
| B | CYS95 |
| B | TYR98 |
| B | CYS153 |
| B | ALA188 |
| A | TYR64 |
| A | PRO85 |
| A | GLY87 |
| A | CYS88 |
| A | TYR91 |
| A | CYS154 |
| A | GLY185 |
| B | CYS70 |
| site_id | AC2 |
| Number of Residues | 15 |
| Details | binding site for residue HCA A 502 |
| Chain | Residue |
| A | ALA65 |
| A | ARG96 |
| A | GLN191 |
| A | GLY424 |
| A | ILE425 |
| A | HIS442 |
| A | ICS503 |
| A | HOH621 |
| A | HOH646 |
| A | HOH659 |
| A | HOH698 |
| A | HOH734 |
| A | HOH735 |
| A | HOH759 |
| A | HOH767 |
| site_id | AC3 |
| Number of Residues | 13 |
| Details | binding site for residue ICS A 503 |
| Chain | Residue |
| A | VAL70 |
| A | ARG96 |
| A | HIS195 |
| A | TYR229 |
| A | CYS275 |
| A | ILE355 |
| A | GLY356 |
| A | GLY357 |
| A | LEU358 |
| A | ARG359 |
| A | PHE381 |
| A | HIS442 |
| A | HCA502 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | binding site for residue FE B 601 |
| Chain | Residue |
| B | ASP353 |
| B | ASP357 |
| B | HOH715 |
| D | ARG108 |
| D | GLU109 |
| D | HOH889 |
| site_id | AC5 |
| Number of Residues | 16 |
| Details | binding site for residue HCA C 501 |
| Chain | Residue |
| C | ALA65 |
| C | ARG96 |
| C | GLN191 |
| C | GLY424 |
| C | ILE425 |
| C | HIS442 |
| C | ICS502 |
| C | HOH616 |
| C | HOH629 |
| C | HOH640 |
| C | HOH677 |
| C | HOH722 |
| C | HOH725 |
| C | HOH767 |
| C | HOH776 |
| D | HOH903 |
| site_id | AC6 |
| Number of Residues | 13 |
| Details | binding site for residue ICS C 502 |
| Chain | Residue |
| C | VAL70 |
| C | ARG96 |
| C | HIS195 |
| C | TYR229 |
| C | CYS275 |
| C | ILE355 |
| C | GLY356 |
| C | GLY357 |
| C | LEU358 |
| C | ARG359 |
| C | PHE381 |
| C | HIS442 |
| C | HCA501 |
| site_id | AC7 |
| Number of Residues | 14 |
| Details | binding site for residue CLF D 601 |
| Chain | Residue |
| C | CYS62 |
| C | TYR64 |
| C | PRO85 |
| C | GLY87 |
| C | CYS88 |
| C | TYR91 |
| C | CYS154 |
| C | GLY185 |
| D | CYS70 |
| D | SER92 |
| D | CYS95 |
| D | TYR98 |
| D | CYS153 |
| D | ALA188 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | binding site for residue FE D 602 |
| Chain | Residue |
| B | ARG108 |
| B | GLU109 |
| B | HOH965 |
| D | ASP353 |
| D | ASP357 |
| D | HOH725 |
Functional Information from PROSITE/UniProt
| site_id | PS00090 |
| Number of Residues | 15 |
| Details | NITROGENASE_1_2 Nitrogenases component 1 alpha and beta subunits signature 2. SECpigliGDDIeSV |
| Chain | Residue | Details |
| A | SER152-VAL166 | |
| B | THR151-PHE165 |
| site_id | PS00699 |
| Number of Residues | 8 |
| Details | NITROGENASE_1_1 Nitrogenases component 1 alpha and beta subunits signature 1. ISHGPVGC |
| Chain | Residue | Details |
| A | ILE81-CYS88 | |
| B | TYR88-CYS95 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | BINDING: |
| Chain | Residue | Details |
| B | CYS70 | |
| C | HIS442 | |
| B | CYS95 | |
| B | CYS153 | |
| B | ALA188 | |
| D | CYS70 | |
| D | CYS95 | |
| D | CYS153 | |
| D | ALA188 | |
| C | CYS275 |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 2 |
| Details | M-CSA 212 |
| Chain | Residue | Details |
| B | CYS153 | metal ligand |
| B | VAL157 | polar interaction, single electron acceptor, single electron donor, single electron relay |
| A | ARG96 | activator, hydrogen bond donor |
| A | HIS195 | activator, polar interaction |
| site_id | MCSA2 |
| Number of Residues | 2 |
| Details | M-CSA 212 |
| Chain | Residue | Details |
| D | CYS153 | metal ligand |
| D | VAL157 | polar interaction, single electron acceptor, single electron donor, single electron relay |
| C | ARG96 | activator, hydrogen bond donor |
| C | HIS195 | activator, polar interaction |
