1FFU
CARBON MONOXIDE DEHYDROGENASE FROM HYDROGENOPHAGA PSEUDOFLAVA WHICH LACKS THE MO-PYRANOPTERIN MOIETY OF THE MOLYBDENUM COFACTOR
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0008805 | molecular_function | carbon-monoxide oxygenase activity |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0051536 | molecular_function | iron-sulfur cluster binding |
| A | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
| B | 0005506 | molecular_function | iron ion binding |
| B | 0005507 | molecular_function | copper ion binding |
| B | 0008805 | molecular_function | carbon-monoxide oxygenase activity |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0018492 | molecular_function | carbon-monoxide dehydrogenase (acceptor) activity |
| B | 0030151 | molecular_function | molybdenum ion binding |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0008805 | molecular_function | carbon-monoxide oxygenase activity |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0018492 | molecular_function | carbon-monoxide dehydrogenase (acceptor) activity |
| C | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| C | 0071949 | molecular_function | FAD binding |
| D | 0008805 | molecular_function | carbon-monoxide oxygenase activity |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0051536 | molecular_function | iron-sulfur cluster binding |
| D | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
| E | 0005506 | molecular_function | iron ion binding |
| E | 0005507 | molecular_function | copper ion binding |
| E | 0008805 | molecular_function | carbon-monoxide oxygenase activity |
| E | 0016491 | molecular_function | oxidoreductase activity |
| E | 0018492 | molecular_function | carbon-monoxide dehydrogenase (acceptor) activity |
| E | 0030151 | molecular_function | molybdenum ion binding |
| E | 0046872 | molecular_function | metal ion binding |
| F | 0008805 | molecular_function | carbon-monoxide oxygenase activity |
| F | 0016491 | molecular_function | oxidoreductase activity |
| F | 0018492 | molecular_function | carbon-monoxide dehydrogenase (acceptor) activity |
| F | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| F | 0071949 | molecular_function | FAD binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE FES A 1907 |
| Chain | Residue |
| A | GLN100 |
| A | CYS101 |
| A | GLY102 |
| A | CYS104 |
| A | CYS136 |
| A | ARG137 |
| A | CYS138 |
| site_id | AC2 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE FES A 1908 |
| Chain | Residue |
| A | SER45 |
| A | HIS46 |
| A | CYS47 |
| A | GLY48 |
| A | CYS50 |
| A | LYS60 |
| A | CYS62 |
| A | GLY41 |
| A | CYS42 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE FES D 1909 |
| Chain | Residue |
| D | GLN100 |
| D | CYS101 |
| D | GLY102 |
| D | CYS104 |
| D | CYS136 |
| D | ARG137 |
| D | CYS138 |
| site_id | AC4 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE FES D 1910 |
| Chain | Residue |
| D | GLY41 |
| D | CYS42 |
| D | SER45 |
| D | HIS46 |
| D | CYS47 |
| D | GLY48 |
| D | CYS50 |
| D | LYS60 |
| D | CYS62 |
| site_id | AC5 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE CDP B 1920 |
| Chain | Residue |
| B | GLN524 |
| B | HIS526 |
| B | THR529 |
| B | SER564 |
| B | ARG565 |
| B | SER566 |
| B | THR567 |
| B | CYS680 |
| B | THR682 |
| B | ILE684 |
| B | ASN685 |
| B | ILE689 |
| B | LYS753 |
| B | GLY754 |
| B | VAL755 |
| B | ALA756 |
| B | HOH2245 |
| B | HOH2395 |
| site_id | AC6 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE CDP E 1921 |
| Chain | Residue |
| E | GLN524 |
| E | HIS526 |
| E | THR529 |
| E | THR561 |
| E | SER564 |
| E | ARG565 |
| E | SER566 |
| E | THR567 |
| E | CYS680 |
| E | THR682 |
| E | ILE684 |
| E | ASN685 |
| E | ILE689 |
| E | LYS753 |
| E | GLY754 |
| E | VAL755 |
| E | ALA756 |
| E | HOH2361 |
| E | HOH2373 |
| site_id | AC7 |
| Number of Residues | 32 |
| Details | BINDING SITE FOR RESIDUE FAD C 1930 |
| Chain | Residue |
| C | HOH2032 |
| C | HOH2055 |
| A | SER45 |
| A | HIS46 |
| C | LYS29 |
| C | LEU30 |
| C | ALA32 |
| C | GLY33 |
| C | GLY34 |
| C | HIS35 |
| C | SER36 |
| C | LEU37 |
| C | ILE54 |
| C | ILE101 |
| C | ALA102 |
| C | GLY110 |
| C | THR111 |
| C | GLY114 |
| C | ASP115 |
| C | ALA117 |
| C | ASN123 |
| C | ASP124 |
| C | LEU161 |
| C | VAL166 |
| C | MET167 |
| C | LYS185 |
| C | GLY191 |
| C | ASP192 |
| C | TRP193 |
| C | HOH1934 |
| C | HOH1988 |
| C | HOH2014 |
| site_id | AC8 |
| Number of Residues | 32 |
| Details | BINDING SITE FOR RESIDUE FAD F 1931 |
| Chain | Residue |
| D | SER45 |
| F | LYS29 |
| F | LEU30 |
| F | ALA32 |
| F | GLY33 |
| F | GLY34 |
| F | HIS35 |
| F | SER36 |
| F | LEU37 |
| F | ALA74 |
| F | ILE101 |
| F | ALA102 |
| F | GLY110 |
| F | THR111 |
| F | GLY114 |
| F | ASP115 |
| F | ALA117 |
| F | HIS118 |
| F | ASN123 |
| F | ASP124 |
| F | LEU161 |
| F | VAL166 |
| F | MET167 |
| F | LYS185 |
| F | GLY191 |
| F | ASP192 |
| F | TRP193 |
| F | HOH1963 |
| F | HOH1969 |
| F | HOH1975 |
| F | HOH2023 |
| F | HOH2027 |
Functional Information from PROSITE/UniProt
| site_id | PS00435 |
| Number of Residues | 11 |
| Details | PEROXIDASE_1 Peroxidases proximal heme-ligand signature. DAKLLAGGHSL |
| Chain | Residue | Details |
| C | ASP27-LEU37 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | BINDING: |
| Chain | Residue | Details |
| B | CSZ385 | |
| D | CYS47 | |
| D | CYS50 | |
| D | CYS62 | |
| D | CYS101 | |
| D | CYS104 | |
| D | CYS136 | |
| D | CYS138 | |
| B | GLU757 | |
| E | CSZ385 | |
| E | GLU757 | |
| A | CYS101 | |
| A | CYS104 | |
| A | CYS136 | |
| A | CYS138 | |
| D | CYS42 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | MOD_RES: 4-hydroxyarginine => ECO:0000269|PubMed:10966817 |
| Chain | Residue | Details |
| B | ARO384 | |
| E | ARO384 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1fiq |
| Chain | Residue | Details |
| B | GLU757 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1fiq |
| Chain | Residue | Details |
| E | GLU757 |
| site_id | CSA3 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1fiq |
| Chain | Residue | Details |
| B | GLN237 |
| site_id | CSA4 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1fiq |
| Chain | Residue | Details |
| E | GLN237 |
