1MIO
X-RAY CRYSTAL STRUCTURE OF THE NITROGENASE MOLYBDENUM-IRON PROTEIN FROM CLOSTRIDIUM PASTEURIANUM AT 3.0 ANGSTROMS RESOLUTION
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 | 6 |
| Details | BINDING SITE FOR RESIDUE CA B 492 |
| Chain | Residue |
| B | PHE60 |
| B | LYS61 |
| B | GLU62 |
| B | TYR420 |
| D | ASP301 |
| D | ASP305 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CA D 492 |
| Chain | Residue |
| D | GLU62 |
| B | ASP301 |
| B | ASP305 |
| D | LYS61 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE HCA B 494 |
| Chain | Residue |
| A | ALA56 |
| A | ARG87 |
| A | GLN182 |
| A | GLY464 |
| A | ILE465 |
| A | GLN480 |
| A | HIS482 |
| B | CFM496 |
| site_id | AC4 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE CFM B 496 |
| Chain | Residue |
| A | VAL61 |
| A | ARG87 |
| A | HIS186 |
| A | TYR216 |
| A | ILE218 |
| A | CYS262 |
| A | SER265 |
| A | VAL343 |
| A | GLY344 |
| A | GLY345 |
| A | ARG347 |
| A | PHE369 |
| A | HIS482 |
| B | HCA494 |
| site_id | AC5 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE CLP B 498 |
| Chain | Residue |
| A | CYS53 |
| A | TYR55 |
| A | PRO76 |
| A | GLY78 |
| A | CYS79 |
| A | CYS145 |
| A | GLY176 |
| B | CYS23 |
| B | PRO25 |
| B | SER45 |
| B | GLY47 |
| B | CYS48 |
| B | HIS52 |
| B | THR105 |
| B | CYS106 |
| B | SER141 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE HCA D 494 |
| Chain | Residue |
| C | GLN182 |
| C | GLY464 |
| C | ILE465 |
| C | LYS466 |
| C | HIS482 |
| D | CFM496 |
| site_id | AC7 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE CFM D 496 |
| Chain | Residue |
| C | VAL61 |
| C | ARG87 |
| C | GLN182 |
| C | HIS186 |
| C | TYR216 |
| C | CYS262 |
| C | SER265 |
| C | VAL343 |
| C | GLY344 |
| C | GLY345 |
| C | ARG347 |
| C | PHE369 |
| C | HIS482 |
| D | HCA494 |
| site_id | AC8 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE CLP D 498 |
| Chain | Residue |
| C | CYS53 |
| C | TYR55 |
| C | PRO76 |
| C | GLY78 |
| C | CYS79 |
| C | CYS145 |
| C | GLY176 |
| D | CYS23 |
| D | PRO25 |
| D | SER45 |
| D | GLY47 |
| D | CYS48 |
| D | TYR51 |
| D | CYS106 |
| D | SER141 |
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. ITHGPIGC |
| Chain | Residue | Details |
| A | ILE72-CYS79 | |
| B | HIS41-CYS48 |
| site_id | PS00090 |
| Number of Residues | 15 |
| Details | NITROGENASE_1_2 Nitrogenases component 1 alpha and beta subunits signature 2. ATCpvgliGDDIlAV |
| Chain | Residue | Details |
| A | ALA143-VAL157 | |
| B | THR104-TYR118 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | BINDING: |
| Chain | Residue | Details |
| B | CYS23 | |
| B | CYS48 | |
| B | CYS106 | |
| B | SER141 | |
| D | CYS23 | |
| D | CYS48 | |
| D | CYS106 | |
| D | SER141 | |
| C | HIS263 | |
| C | SER483 |
