6OP3
Selenium incorporated FeMo-cofactor of nitrogenase from Azotobacter vinelandii with low concentration of selenium
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| 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 | carbonyl sulfide nitrogenase activity |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0051536 | molecular_function | iron-sulfur cluster binding |
| B | 0000166 | molecular_function | nucleotide 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 | carbonyl sulfide nitrogenase activity |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0051536 | molecular_function | iron-sulfur cluster binding |
| C | 0000166 | molecular_function | nucleotide 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 | carbonyl sulfide nitrogenase activity |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0051536 | molecular_function | iron-sulfur cluster binding |
| D | 0000166 | molecular_function | nucleotide 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 | 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 | 16 |
| Details | binding site for residue HCA A 501 |
| Chain | Residue |
| A | ALA65 |
| A | HOH723 |
| A | HOH758 |
| A | HOH843 |
| A | HOH856 |
| A | HOH858 |
| B | HOH725 |
| B | HOH817 |
| A | GLN191 |
| A | GLY424 |
| A | ILE425 |
| A | HIS442 |
| A | ICS502 |
| A | HOH614 |
| A | HOH697 |
| A | HOH718 |
| site_id | AC2 |
| Number of Residues | 11 |
| Details | binding site for residue ICS A 502 |
| Chain | Residue |
| A | VAL70 |
| A | ARG96 |
| A | TYR229 |
| A | CYS275 |
| A | GLY356 |
| A | GLY357 |
| A | LEU358 |
| A | ARG359 |
| A | HIS442 |
| A | HCA501 |
| A | SE505 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | binding site for residue IMD A 503 |
| Chain | Residue |
| A | GLU287 |
| A | TRP294 |
| A | HOH872 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | binding site for residue IMD A 504 |
| Chain | Residue |
| A | ARG96 |
| A | ASN98 |
| A | TYR99 |
| A | THR111 |
| D | HOH830 |
| D | HOH1013 |
| D | HOH1098 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | binding site for residue SE A 505 |
| Chain | Residue |
| A | VAL70 |
| A | HIS195 |
| A | PHE381 |
| A | ICS502 |
| site_id | AC6 |
| Number of Residues | 14 |
| Details | binding site for residue CLF B 601 |
| Chain | Residue |
| A | CYS62 |
| A | TYR64 |
| A | PRO85 |
| A | GLY87 |
| A | CYS88 |
| A | TYR91 |
| A | CYS154 |
| A | GLY185 |
| B | CYS70 |
| B | SER92 |
| B | CYS95 |
| B | TYR98 |
| B | CYS153 |
| B | SER188 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | binding site for residue IMD B 602 |
| Chain | Residue |
| B | SER482 |
| B | THR483 |
| B | GLN492 |
| B | THR496 |
| B | HOH736 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | binding site for residue IMD B 603 |
| Chain | Residue |
| A | GLY157 |
| B | GLU120 |
| B | ALA123 |
| C | GLN41 |
| C | LYS44 |
| site_id | AC9 |
| Number of Residues | 3 |
| Details | binding site for residue MG B 604 |
| Chain | Residue |
| B | HOH911 |
| B | HOH1033 |
| B | HOH1289 |
| site_id | AD1 |
| Number of Residues | 6 |
| Details | binding site for residue IMD B 605 |
| Chain | Residue |
| B | LEU253 |
| B | ASP256 |
| B | GLY275 |
| B | THR276 |
| B | GLU280 |
| B | HOH973 |
| site_id | AD2 |
| Number of Residues | 5 |
| Details | binding site for residue IMD B 606 |
| Chain | Residue |
| B | GLN513 |
| B | ALA514 |
| B | HOH994 |
| D | PHE15 |
| D | LEU24 |
| site_id | AD3 |
| Number of Residues | 6 |
| Details | binding site for residue CA B 607 |
| Chain | Residue |
| B | ASP353 |
| B | ASP357 |
| B | HOH764 |
| D | ARG108 |
| D | GLU109 |
| D | HOH1018 |
| site_id | AD4 |
| Number of Residues | 17 |
| Details | binding site for residue HCA C 501 |
| Chain | Residue |
| C | HOH878 |
| D | HOH731 |
| D | HOH852 |
| C | ALA65 |
| C | GLN191 |
| C | GLY424 |
| C | ILE425 |
| C | HIS442 |
| C | ICS502 |
| C | HOH618 |
| C | HOH634 |
| C | HOH699 |
| C | HOH729 |
| C | HOH814 |
| C | HOH837 |
| C | HOH841 |
| C | HOH876 |
| site_id | AD5 |
| Number of Residues | 11 |
| Details | binding site for residue ICS C 502 |
| Chain | Residue |
| C | VAL70 |
| C | ARG96 |
| C | TYR229 |
| C | CYS275 |
| C | GLY356 |
| C | GLY357 |
| C | LEU358 |
| C | ARG359 |
| C | HIS442 |
| C | HCA501 |
| C | SE504 |
| site_id | AD6 |
| Number of Residues | 3 |
| Details | binding site for residue IMD C 503 |
| Chain | Residue |
| C | TRP294 |
| C | HOH632 |
| C | HOH812 |
| site_id | AD7 |
| Number of Residues | 4 |
| Details | binding site for residue SE C 504 |
| Chain | Residue |
| C | VAL70 |
| C | HIS195 |
| C | PHE381 |
| C | ICS502 |
| site_id | AD8 |
| Number of Residues | 7 |
| Details | binding site for residue IMD C 505 |
| Chain | Residue |
| B | HOH989 |
| B | HOH1076 |
| C | ARG96 |
| C | ASN98 |
| C | TYR99 |
| C | THR111 |
| C | HOH601 |
| site_id | AD9 |
| Number of Residues | 1 |
| Details | binding site for residue CA C 506 |
| Chain | Residue |
| C | LYS332 |
| site_id | AE1 |
| Number of Residues | 5 |
| Details | binding site for residue IMD D 601 |
| Chain | Residue |
| A | LYS44 |
| C | GLY157 |
| C | PHE186 |
| D | GLU120 |
| D | ALA123 |
| site_id | AE2 |
| Number of Residues | 14 |
| Details | binding site for residue CLF D 602 |
| 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 | SER188 |
| site_id | AE3 |
| Number of Residues | 5 |
| Details | binding site for residue IMD D 603 |
| Chain | Residue |
| D | SER482 |
| D | THR483 |
| D | GLN492 |
| D | THR496 |
| D | HOH754 |
| site_id | AE4 |
| Number of Residues | 6 |
| Details | binding site for residue IMD D 604 |
| Chain | Residue |
| D | LEU253 |
| D | ASP256 |
| D | GLY275 |
| D | THR276 |
| D | GLU280 |
| D | HOH989 |
| site_id | AE5 |
| Number of Residues | 2 |
| Details | binding site for residue MG D 605 |
| Chain | Residue |
| D | LYS9 |
| D | HOH791 |
| site_id | AE6 |
| Number of Residues | 4 |
| Details | binding site for residue IMD D 606 |
| Chain | Residue |
| D | GLN513 |
| D | ALA514 |
| D | HOH702 |
| D | HOH1012 |
| site_id | AE7 |
| Number of Residues | 6 |
| Details | binding site for residue CA D 607 |
| Chain | Residue |
| A | PHE429 |
| B | ARG108 |
| B | GLU109 |
| D | ASP353 |
| D | ASP357 |
| D | CA608 |
| site_id | AE8 |
| Number of Residues | 6 |
| Details | binding site for residue CA D 608 |
| Chain | Residue |
| B | ARG108 |
| B | GLU109 |
| B | HOH1028 |
| D | ASP353 |
| D | ASP357 |
| D | CA607 |
Functional Information from PROSITE/UniProt
| site_id | PS00699 |
| Number of Residues | 8 |
| Details | NITROGENASE_1_1 Nitrogenases component 1 alpha and beta subunits signature 1. YVHGSQGC |
| Chain | Residue | Details |
| B | TYR88-CYS95 | |
| A | ILE81-CYS88 |
| site_id | PS00090 |
| Number of Residues | 15 |
| Details | NITROGENASE_1_2 Nitrogenases component 1 alpha and beta subunits signature 2. TTCmaeviGDDLnAF |
| Chain | Residue | Details |
| B | THR151-PHE165 | |
| A | SER152-VAL166 |
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 | SER188 | |
| D | CYS70 | |
| D | CYS95 | |
| D | CYS153 | |
| D | SER188 | |
| 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 |
