1B25
FORMALDEHYDE FERREDOXIN OXIDOREDUCTASE FROM PYROCOCCUS FURIOSUS
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0009055 | molecular_function | electron transfer activity |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016625 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, iron-sulfur protein as acceptor |
| A | 0033726 | molecular_function | aldehyde ferredoxin oxidoreductase activity |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0051536 | molecular_function | iron-sulfur cluster binding |
| A | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
| B | 0009055 | molecular_function | electron transfer activity |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016625 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, iron-sulfur protein as acceptor |
| B | 0033726 | molecular_function | aldehyde ferredoxin oxidoreductase activity |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0051536 | molecular_function | iron-sulfur cluster binding |
| B | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
| C | 0009055 | molecular_function | electron transfer activity |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0016625 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, iron-sulfur protein as acceptor |
| C | 0033726 | molecular_function | aldehyde ferredoxin oxidoreductase activity |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0051536 | molecular_function | iron-sulfur cluster binding |
| C | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
| D | 0009055 | molecular_function | electron transfer activity |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0016625 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, iron-sulfur protein as acceptor |
| D | 0033726 | molecular_function | aldehyde ferredoxin oxidoreductase activity |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0051536 | molecular_function | iron-sulfur cluster binding |
| D | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
Functional Information from PDB Data
| site_id | 1A |
| Number of Residues | 1 |
| Details | FIRST MOLYBDOPTERIN BINDING MOTIF |
| Chain | Residue |
| A | ASP333 |
| site_id | 1B |
| Number of Residues | 1 |
| Details | FIRST MOLYBDOPTERIN BINDING MOTIF |
| Chain | Residue |
| B | GLU486 |
| site_id | 1C |
| Number of Residues | 1 |
| Details | FIRST MOLYBDOPTERIN BINDING MOTIF |
| Chain | Residue |
| C | ASP333 |
| site_id | 1D |
| Number of Residues | 1 |
| Details | FIRST MOLYBDOPTERIN BINDING MOTIF |
| Chain | Residue |
| D | ASP333 |
| site_id | 2A |
| Number of Residues | 1 |
| Details | SECOND MOLYBDOPTERIN BINDING MOTIF |
| Chain | Residue |
| A | GLU486 |
| site_id | 2B |
| Number of Residues | 1 |
| Details | SECOND MOLYBDOPTERIN BINDING MOTIF |
| Chain | Residue |
| B | GLU486 |
| site_id | 2C |
| Number of Residues | 1 |
| Details | SECOND MOLYBDOPTERIN BINDING MOTIF |
| Chain | Residue |
| C | GLU486 |
| site_id | 2D |
| Number of Residues | 1 |
| Details | SECOND MOLYBDOPTERIN BINDING MOTIF |
| Chain | Residue |
| D | GLU486 |
| site_id | AC1 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE SF4 A 700 |
| Chain | Residue |
| A | LYS75 |
| A | ARG180 |
| A | GLY283 |
| A | CYS284 |
| A | CYS287 |
| A | MET289 |
| A | CYS291 |
| A | CYS491 |
| A | PTT800 |
| A | SER72 |
| site_id | AC2 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE SF4 B 701 |
| Chain | Residue |
| B | SER72 |
| B | LYS75 |
| B | ARG180 |
| B | GLY283 |
| B | CYS284 |
| B | CYS287 |
| B | MET289 |
| B | CYS291 |
| B | CYS491 |
| B | PTT801 |
| site_id | AC3 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE SF4 C 702 |
| Chain | Residue |
| C | SER72 |
| C | LYS75 |
| C | ARG180 |
| C | GLY283 |
| C | CYS284 |
| C | CYS287 |
| C | MET289 |
| C | PRO290 |
| C | CYS291 |
| C | CYS491 |
| C | PTT802 |
| site_id | AC4 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE SF4 D 703 |
| Chain | Residue |
| D | SER72 |
| D | LYS75 |
| D | ARG180 |
| D | GLY283 |
| D | CYS284 |
| D | CYS287 |
| D | MET289 |
| D | PRO290 |
| D | CYS291 |
| D | CYS491 |
| D | PTT803 |
| site_id | AC5 |
| Number of Residues | 39 |
| Details | BINDING SITE FOR RESIDUE PTT A 800 |
| Chain | Residue |
| A | LYS75 |
| A | GLY91 |
| A | ASN92 |
| A | LEU93 |
| A | GLY94 |
| A | GLY179 |
| A | ARG180 |
| A | ALA181 |
| A | ALA182 |
| A | GLY183 |
| A | ARG184 |
| A | THR240 |
| A | GLU304 |
| A | ASP306 |
| A | TYR307 |
| A | GLU308 |
| A | ASN309 |
| A | ASP333 |
| A | MET337 |
| A | ASP338 |
| A | THR339 |
| A | HIS436 |
| A | HIS437 |
| A | LYS438 |
| A | PHE485 |
| A | GLU486 |
| A | ALA490 |
| A | CYS491 |
| A | ARG492 |
| A | LEU493 |
| A | SF4700 |
| A | HOH806 |
| A | HOH808 |
| A | HOH809 |
| A | HOH814 |
| A | HOH1082 |
| A | HOH1083 |
| A | HOH1084 |
| A | HOH1085 |
| site_id | AC6 |
| Number of Residues | 38 |
| Details | BINDING SITE FOR RESIDUE PTT B 801 |
| Chain | Residue |
| B | ARG184 |
| B | THR240 |
| B | GLU304 |
| B | ASP306 |
| B | TYR307 |
| B | GLU308 |
| B | ASN309 |
| B | ASP333 |
| B | MET337 |
| B | ASP338 |
| B | THR339 |
| B | HIS436 |
| B | HIS437 |
| B | LYS438 |
| B | PHE485 |
| B | GLU486 |
| B | ALA490 |
| B | CYS491 |
| B | ARG492 |
| B | SF4701 |
| B | HOH803 |
| B | HOH806 |
| B | HOH808 |
| B | HOH809 |
| B | HOH1116 |
| B | HOH1117 |
| B | HOH1118 |
| B | HOH1119 |
| B | LYS75 |
| B | GLY91 |
| B | ASN92 |
| B | LEU93 |
| B | GLY94 |
| B | GLY179 |
| B | ARG180 |
| B | ALA181 |
| B | ALA182 |
| B | GLY183 |
| site_id | AC7 |
| Number of Residues | 39 |
| Details | BINDING SITE FOR RESIDUE PTT C 802 |
| Chain | Residue |
| C | LYS75 |
| C | GLY91 |
| C | ASN92 |
| C | LEU93 |
| C | GLY94 |
| C | GLY179 |
| C | ARG180 |
| C | ALA181 |
| C | ALA182 |
| C | GLY183 |
| C | ARG184 |
| C | THR240 |
| C | GLU304 |
| C | ASP306 |
| C | TYR307 |
| C | GLU308 |
| C | ASN309 |
| C | ASP333 |
| C | MET337 |
| C | ASP338 |
| C | THR339 |
| C | HIS436 |
| C | HIS437 |
| C | LYS438 |
| C | PHE485 |
| C | GLU486 |
| C | ALA490 |
| C | CYS491 |
| C | ARG492 |
| C | LEU493 |
| C | SF4702 |
| C | HOH806 |
| C | HOH810 |
| C | HOH816 |
| C | HOH839 |
| C | HOH1192 |
| C | HOH1193 |
| C | HOH1194 |
| C | HOH1195 |
| site_id | AC8 |
| Number of Residues | 39 |
| Details | BINDING SITE FOR RESIDUE PTT D 803 |
| Chain | Residue |
| D | LYS75 |
| D | GLY91 |
| D | ASN92 |
| D | LEU93 |
| D | GLY94 |
| D | GLY179 |
| D | ARG180 |
| D | ALA181 |
| D | ALA182 |
| D | GLY183 |
| D | ARG184 |
| D | THR240 |
| D | GLU304 |
| D | ASP306 |
| D | TYR307 |
| D | GLU308 |
| D | ASN309 |
| D | ALA332 |
| D | ASP333 |
| D | MET337 |
| D | ASP338 |
| D | THR339 |
| D | HIS436 |
| D | HIS437 |
| D | LYS438 |
| D | PHE485 |
| D | GLU486 |
| D | ALA490 |
| D | CYS491 |
| D | ARG492 |
| D | SF4703 |
| D | HOH806 |
| D | HOH808 |
| D | HOH812 |
| D | HOH813 |
| D | HOH1153 |
| D | HOH1154 |
| D | HOH1155 |
| D | HOH1156 |
