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 | PS00090 |
Number of Residues | 15 |
Details | NITROGENASE_1_2 Nitrogenases component 1 alpha and beta subunits signature 2. TTClsetlGDDLpTY |
Chain | Residue | Details |
B | THR104-TYR118 | |
A | ALA143-VAL157 |
site_id | PS00699 |
Number of Residues | 8 |
Details | NITROGENASE_1_1 Nitrogenases component 1 alpha and beta subunits signature 1. HSHGSQGC |
Chain | Residue | Details |
B | HIS41-CYS48 | |
A | ILE72-CYS79 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 8 |
Details | BINDING: |
Chain | Residue | Details |
B | CYS23 | |
C | SER483 | |
B | CYS48 | |
B | CYS106 | |
B | SER141 | |
D | CYS23 | |
D | CYS48 | |
D | CYS106 | |
D | SER141 | |
C | HIS263 |