1FP4
CRYSTAL STRUCTURE OF THE ALPHA-H195Q MUTANT OF NITROGENASE
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 | 5 |
Details | BINDING SITE FOR RESIDUE CA D 524 |
Chain | Residue |
A | LYS433 |
B | ARG108 |
B | GLU109 |
D | ASP353 |
D | ASP357 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CA B 524 |
Chain | Residue |
D | GLU109 |
B | ASP353 |
B | ASP357 |
C | LYS433 |
D | ARG108 |
site_id | AC3 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE HCA A 494 |
Chain | Residue |
A | ALA65 |
A | ARG96 |
A | GLN191 |
A | GLY424 |
A | ILE425 |
A | HIS442 |
A | CFM496 |
A | HOH507 |
site_id | AC4 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE HCA C 495 |
Chain | Residue |
C | ALA65 |
C | ARG96 |
C | GLN191 |
C | GLY424 |
C | ILE425 |
C | HIS442 |
C | CFM497 |
C | HOH506 |
C | HOH545 |
C | HOH555 |
site_id | AC5 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE CFM A 496 |
Chain | Residue |
A | VAL70 |
A | ARG96 |
A | GLN195 |
A | TYR229 |
A | ILE231 |
A | CYS275 |
A | SER278 |
A | ILE355 |
A | GLY356 |
A | GLY357 |
A | LEU358 |
A | ARG359 |
A | PHE381 |
A | HIS442 |
A | HCA494 |
A | HOH551 |
site_id | AC6 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE CFM C 497 |
Chain | Residue |
C | VAL70 |
C | ARG96 |
C | GLN195 |
C | TYR229 |
C | ILE231 |
C | CYS275 |
C | SER278 |
C | ILE355 |
C | GLY356 |
C | GLY357 |
C | LEU358 |
C | ARG359 |
C | PHE381 |
C | HIS442 |
C | HCA495 |
C | HOH545 |
site_id | AC7 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE CLP A 498 |
Chain | Residue |
A | CYS62 |
A | TYR64 |
A | PRO85 |
A | GLY87 |
A | CYS88 |
A | TYR91 |
A | CYS154 |
A | GLY185 |
B | CYS70 |
B | PRO72 |
B | SER92 |
B | CYS95 |
B | TYR98 |
B | CYS153 |
B | SER188 |
site_id | AC8 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE CLP C 499 |
Chain | Residue |
C | CYS62 |
C | TYR64 |
C | PRO85 |
C | GLY87 |
C | CYS88 |
C | TYR91 |
C | CYS154 |
C | GLY185 |
D | CYS70 |
D | PRO72 |
D | SER92 |
D | CYS95 |
D | TYR98 |
D | CYS153 |
D | SER188 |
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 | 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 | GLN195 | 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 | GLN195 | activator, polar interaction |