6T7J
As-isolated Ni-free crystal structure of carbon monoxide dehydrogenase from Thermococcus sp. AM4 produced without CooC maturase
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003824 | molecular_function | catalytic activity |
A | 0004601 | molecular_function | peroxidase activity |
A | 0006091 | biological_process | generation of precursor metabolites and energy |
A | 0016151 | molecular_function | nickel cation binding |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0042542 | biological_process | response to hydrogen peroxide |
A | 0043885 | molecular_function | anaerobic carbon-monoxide dehydrogenase activity |
A | 0046872 | molecular_function | metal ion binding |
A | 0050418 | molecular_function | hydroxylamine reductase activity |
A | 0051536 | molecular_function | iron-sulfur cluster binding |
A | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
A | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
A | 0098869 | biological_process | cellular oxidant detoxification |
B | 0003824 | molecular_function | catalytic activity |
B | 0004601 | molecular_function | peroxidase activity |
B | 0006091 | biological_process | generation of precursor metabolites and energy |
B | 0016151 | molecular_function | nickel cation binding |
B | 0016491 | molecular_function | oxidoreductase activity |
B | 0042542 | biological_process | response to hydrogen peroxide |
B | 0043885 | molecular_function | anaerobic carbon-monoxide dehydrogenase activity |
B | 0046872 | molecular_function | metal ion binding |
B | 0050418 | molecular_function | hydroxylamine reductase activity |
B | 0051536 | molecular_function | iron-sulfur cluster binding |
B | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
B | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
B | 0098869 | biological_process | cellular oxidant detoxification |
D | 0003824 | molecular_function | catalytic activity |
D | 0004601 | molecular_function | peroxidase activity |
D | 0006091 | biological_process | generation of precursor metabolites and energy |
D | 0016151 | molecular_function | nickel cation binding |
D | 0016491 | molecular_function | oxidoreductase activity |
D | 0042542 | biological_process | response to hydrogen peroxide |
D | 0043885 | molecular_function | anaerobic carbon-monoxide dehydrogenase activity |
D | 0046872 | molecular_function | metal ion binding |
D | 0050418 | molecular_function | hydroxylamine reductase activity |
D | 0051536 | molecular_function | iron-sulfur cluster binding |
D | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
D | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
D | 0098869 | biological_process | cellular oxidant detoxification |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 7 |
Details | binding site for residue SF4 B 701 |
Chain | Residue |
B | CYS55 |
B | CYS58 |
B | MET60 |
B | GLY61 |
B | CYS63 |
B | CYS77 |
B | ARG87 |
site_id | AC2 |
Number of Residues | 5 |
Details | binding site for residue FES B 702 |
Chain | Residue |
B | CYS54 |
B | ARG56 |
B | ARG64 |
B | CYS46 |
B | GLY49 |
site_id | AC3 |
Number of Residues | 10 |
Details | binding site for residue MSK B 703 |
Chain | Residue |
B | HIS269 |
B | CYS305 |
B | PHE322 |
B | CYS343 |
B | GLY450 |
B | CYS451 |
B | CYS481 |
B | CYS522 |
B | MET556 |
B | SER557 |
site_id | AC4 |
Number of Residues | 6 |
Details | binding site for residue PO4 B 704 |
Chain | Residue |
A | LYS258 |
A | LYS410 |
B | GLU22 |
B | HIS409 |
B | HOH802 |
B | HOH830 |
site_id | AC5 |
Number of Residues | 6 |
Details | binding site for residue BU3 B 705 |
Chain | Residue |
B | THR361 |
B | HIS367 |
B | ILE368 |
B | ALA371 |
B | HIS373 |
B | LEU632 |
site_id | AC6 |
Number of Residues | 4 |
Details | binding site for residue BU3 B 706 |
Chain | Residue |
B | ARG438 |
B | LEU539 |
B | LEU628 |
B | TRP630 |
site_id | AC7 |
Number of Residues | 6 |
Details | binding site for residue BU3 B 707 |
Chain | Residue |
A | PO4704 |
A | CIT705 |
B | LYS258 |
B | GLU259 |
B | ASP260 |
B | TYR261 |
site_id | AC8 |
Number of Residues | 2 |
Details | binding site for residue PEG B 708 |
Chain | Residue |
B | THR593 |
B | LYS603 |
site_id | AC9 |
Number of Residues | 10 |
Details | binding site for residue SF4 A 701 |
Chain | Residue |
A | CYS55 |
A | ASN57 |
A | CYS58 |
A | MET60 |
A | GLY61 |
A | CYS63 |
A | VAL76 |
A | CYS77 |
A | ARG87 |
A | ILE206 |
site_id | AD1 |
Number of Residues | 4 |
Details | binding site for residue FES A 702 |
Chain | Residue |
A | CYS46 |
A | CYS54 |
D | ARG56 |
D | FES702 |
site_id | AD2 |
Number of Residues | 11 |
Details | binding site for residue MSK A 703 |
Chain | Residue |
A | HIS269 |
A | CYS304 |
A | CYS305 |
A | PHE322 |
A | CYS343 |
A | GLY450 |
A | CYS451 |
A | CYS481 |
A | CYS522 |
A | MET556 |
A | SER557 |
site_id | AD3 |
Number of Residues | 3 |
Details | binding site for residue PO4 A 704 |
Chain | Residue |
A | HIS409 |
B | GLU259 |
B | BU3707 |
site_id | AD4 |
Number of Residues | 7 |
Details | binding site for residue CIT A 705 |
Chain | Residue |
A | LYS18 |
A | GLY19 |
A | GLU22 |
A | HIS409 |
B | ASP260 |
B | LYS296 |
B | BU3707 |
site_id | AD5 |
Number of Residues | 9 |
Details | binding site for residue SF4 D 701 |
Chain | Residue |
D | CYS55 |
D | CYS58 |
D | MET60 |
D | GLY61 |
D | CYS63 |
D | VAL76 |
D | CYS77 |
D | ARG87 |
D | ILE206 |
site_id | AD6 |
Number of Residues | 5 |
Details | binding site for residue FES D 702 |
Chain | Residue |
A | CYS54 |
A | FES702 |
D | CYS46 |
D | CYS54 |
D | ARG56 |
site_id | AD7 |
Number of Residues | 9 |
Details | binding site for residue MSK D 703 |
Chain | Residue |
D | GLY450 |
D | CYS451 |
D | CYS481 |
D | CYS522 |
D | MET556 |
D | HIS269 |
D | CYS305 |
D | PHE322 |
D | CYS343 |
site_id | AD8 |
Number of Residues | 3 |
Details | binding site for residue PO4 D 704 |
Chain | Residue |
D | GLY187 |
D | SER214 |
D | ARG221 |
site_id | AD9 |
Number of Residues | 4 |
Details | binding site for residue PO4 D 705 |
Chain | Residue |
D | LYS18 |
D | GLU22 |
D | LYS296 |
D | HIS409 |