4XPI
Fe protein independent substrate reduction by nitrogenase variants altered in intramolecular electron transfer
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 | 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 | 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 | 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 | 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 HCA A 501 |
Chain | Residue |
A | ALA65 |
A | HOH722 |
A | HOH729 |
A | HOH743 |
A | HOH745 |
B | HOH824 |
A | GLN191 |
A | GLY424 |
A | ILE425 |
A | HIS442 |
A | ICS502 |
A | HOH622 |
A | HOH634 |
A | HOH651 |
site_id | AC2 |
Number of Residues | 10 |
Details | binding site for residue ICS A 502 |
Chain | Residue |
A | ARG96 |
A | HIS195 |
A | TYR229 |
A | CYS275 |
A | GLY356 |
A | GLY357 |
A | ARG359 |
A | PHE381 |
A | HIS442 |
A | HCA501 |
site_id | AC3 |
Number of Residues | 7 |
Details | binding site for residue GOL A 503 |
Chain | Residue |
A | SER48 |
A | ASN49 |
A | HIS383 |
A | ASN384 |
A | HOH607 |
A | HOH639 |
A | HOH784 |
site_id | AC4 |
Number of Residues | 9 |
Details | binding site for residue 1CL A 504 |
Chain | Residue |
A | CYS62 |
A | GLY87 |
A | CYS88 |
A | CYS154 |
B | CYS70 |
B | SER92 |
B | CYS95 |
B | CYS153 |
B | SER188 |
site_id | AC5 |
Number of Residues | 6 |
Details | binding site for residue CA B 601 |
Chain | Residue |
B | ASP353 |
B | ASP357 |
B | HOH728 |
D | ARG108 |
D | GLU109 |
D | HOH730 |
site_id | AC6 |
Number of Residues | 1 |
Details | binding site for residue GOL B 602 |
Chain | Residue |
B | LYS400 |
site_id | AC7 |
Number of Residues | 7 |
Details | binding site for residue GOL B 603 |
Chain | Residue |
A | ILE101 |
B | PHE15 |
B | LYS21 |
B | HOH849 |
B | HOH875 |
D | GLN513 |
D | ALA514 |
site_id | AC8 |
Number of Residues | 3 |
Details | binding site for residue TRS B 604 |
Chain | Residue |
B | THR49 |
B | LYS50 |
B | GLU51 |
site_id | AC9 |
Number of Residues | 8 |
Details | binding site for residue GOL B 605 |
Chain | Residue |
B | SER482 |
B | THR483 |
B | THR484 |
B | GLY489 |
B | GLN492 |
B | ILE493 |
B | THR496 |
B | HOH829 |
site_id | AD1 |
Number of Residues | 8 |
Details | binding site for residue GOL B 606 |
Chain | Residue |
B | PHE230 |
B | GLU231 |
B | THR232 |
B | TYR233 |
B | GLY470 |
B | PHE471 |
B | GOL607 |
B | HOH727 |
site_id | AD2 |
Number of Residues | 10 |
Details | binding site for residue GOL B 607 |
Chain | Residue |
B | GLU231 |
B | TYR233 |
B | ASN236 |
B | GLN294 |
B | ILE318 |
B | MET320 |
B | PHE375 |
B | THR484 |
B | LEU485 |
B | GOL606 |
site_id | AD3 |
Number of Residues | 8 |
Details | binding site for residue GOL B 608 |
Chain | Residue |
A | ARG93 |
A | THR104 |
A | THR111 |
A | MET112 |
B | ASN65 |
B | PHE450 |
B | ARG453 |
B | ASP454 |
site_id | AD4 |
Number of Residues | 6 |
Details | binding site for residue CA B 609 |
Chain | Residue |
B | ARG108 |
B | GLU109 |
B | HOH789 |
D | ASP353 |
D | ASP357 |
D | HOH720 |
site_id | AD5 |
Number of Residues | 17 |
Details | binding site for residue HCA C 501 |
Chain | Residue |
C | GLN191 |
C | GLY424 |
C | ILE425 |
C | HIS442 |
C | ICS502 |
C | HOH656 |
C | HOH666 |
C | HOH689 |
C | HOH695 |
C | HOH739 |
C | HOH751 |
C | HOH752 |
C | HOH758 |
C | HOH763 |
D | HOH745 |
C | ALA65 |
C | ARG96 |
site_id | AD6 |
Number of Residues | 12 |
Details | binding site for residue ICS C 502 |
Chain | Residue |
C | ARG96 |
C | HIS195 |
C | TYR229 |
C | CYS275 |
C | GLY356 |
C | GLY357 |
C | LEU358 |
C | ARG359 |
C | PHE381 |
C | HIS442 |
C | HCA501 |
C | HOH765 |
site_id | AD7 |
Number of Residues | 5 |
Details | binding site for residue GOL C 503 |
Chain | Residue |
C | HIS196 |
C | ASP200 |
C | ARG203 |
C | HOH619 |
C | HOH660 |
site_id | AD8 |
Number of Residues | 1 |
Details | binding site for residue GOL C 504 |
Chain | Residue |
C | HOH601 |
site_id | AD9 |
Number of Residues | 12 |
Details | binding site for residue GOL C 505 |
Chain | Residue |
C | LYS68 |
C | SER92 |
C | ARG93 |
C | ALA94 |
C | ARG96 |
C | ASN98 |
C | VAL110 |
C | THR111 |
C | MET112 |
C | GOL506 |
C | HOH665 |
C | HOH711 |
site_id | AE1 |
Number of Residues | 8 |
Details | binding site for residue GOL C 506 |
Chain | Residue |
B | HIS519 |
B | HOH882 |
C | ARG96 |
C | ASN98 |
C | TYR99 |
C | THR111 |
C | GOL505 |
C | HOH671 |
site_id | AE2 |
Number of Residues | 5 |
Details | binding site for residue GOL C 507 |
Chain | Residue |
C | LYS133 |
C | THR140 |
C | HOH690 |
D | LEU55 |
D | GLN58 |
site_id | AE3 |
Number of Residues | 7 |
Details | binding site for residue GOL C 508 |
Chain | Residue |
C | SER52 |
C | GLN53 |
C | LEU56 |
C | THR58 |
C | ASP403 |
C | THR405 |
C | HOH694 |
site_id | AE4 |
Number of Residues | 9 |
Details | binding site for residue 1CL C 509 |
Chain | Residue |
C | CYS62 |
C | GLY87 |
C | CYS88 |
C | CYS154 |
D | CYS70 |
D | SER92 |
D | CYS95 |
D | CYS153 |
D | SER188 |
site_id | AE5 |
Number of Residues | 1 |
Details | binding site for residue GOL D 601 |
Chain | Residue |
D | GLU508 |
site_id | AE6 |
Number of Residues | 3 |
Details | binding site for residue TRS D 602 |
Chain | Residue |
D | THR49 |
D | LYS50 |
D | GLU51 |
site_id | AE7 |
Number of Residues | 8 |
Details | binding site for residue GOL D 603 |
Chain | Residue |
D | PHE230 |
D | GLU231 |
D | THR232 |
D | TYR233 |
D | PHE375 |
D | PHE471 |
D | HOH721 |
D | HOH779 |
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. TTCmaeviGDDLnAF |
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. YVHGSQGC |
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 |
C | CYS275 | |
C | HIS442 | |
B | CYS70 | |
B | CYS95 | |
B | CYS153 | |
B | SER188 | |
D | CYS70 | |
D | CYS95 | |
D | CYS153 | |
D | SER188 |
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 |