1B4N
FORMALDEHYDE FERREDOXIN OXIDOREDUCTASE FROM PYROCOCCUS FURIOSUS, COMPLEXED WITH GLUTARATE
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 | A1 |
| Number of Residues | 1 |
| Details | FIRST MOLYBDOPTERIN BINDING MOTIF |
| Chain | Residue |
| A | ASP333 |
| site_id | A2 |
| Number of Residues | 1 |
| Details | SECOND MOLYBDOPTERIN BINDING MOTIF |
| Chain | Residue |
| A | GLU486 |
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA A 620 |
| Chain | Residue |
| A | GLU304 |
| A | ASP306 |
| A | PTE623 |
| A | HOH660 |
| A | HOH661 |
| A | GLY179 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA B 620 |
| Chain | Residue |
| B | GLY179 |
| B | GLU304 |
| B | ASP306 |
| B | PTE623 |
| B | HOH668 |
| B | HOH669 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA C 620 |
| Chain | Residue |
| C | GLY179 |
| C | GLU304 |
| C | ASP306 |
| C | PTE623 |
| C | HOH671 |
| C | HOH672 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA D 620 |
| Chain | Residue |
| D | GLY179 |
| D | GLU304 |
| D | ASP306 |
| D | PTE623 |
| D | HOH673 |
| D | HOH674 |
| site_id | AC5 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE SF4 A 621 |
| Chain | Residue |
| A | SER72 |
| A | LYS75 |
| A | GLY283 |
| A | CYS284 |
| A | CYS287 |
| A | MET289 |
| A | CYS291 |
| A | CYS491 |
| A | PTE623 |
| site_id | AC6 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE GUA A 622 |
| Chain | Residue |
| A | TYR307 |
| A | GLU308 |
| A | TYR416 |
| A | HIS437 |
| A | ARG481 |
| A | ARG492 |
| A | LEU493 |
| A | VAL496 |
| A | PTE623 |
| A | HOH631 |
| site_id | AC7 |
| Number of Residues | 38 |
| Details | BINDING SITE FOR RESIDUE PTE A 623 |
| 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 | ASP306 |
| A | GLU308 |
| A | ASN309 |
| A | ASP333 |
| A | MET337 |
| A | ASP338 |
| A | THR339 |
| A | ILE340 |
| A | HIS436 |
| A | HIS437 |
| A | LYS438 |
| A | PHE485 |
| A | GLU486 |
| A | ALA490 |
| A | CYS491 |
| A | ARG492 |
| A | CA620 |
| A | SF4621 |
| A | GUA622 |
| A | HOH632 |
| A | HOH640 |
| A | HOH650 |
| A | HOH657 |
| A | HOH658 |
| A | HOH659 |
| A | HOH660 |
| A | HOH661 |
| site_id | AC8 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SF4 B 621 |
| Chain | Residue |
| B | SER72 |
| B | LYS75 |
| B | GLY283 |
| B | CYS284 |
| B | CYS287 |
| B | CYS291 |
| B | CYS491 |
| B | PTE623 |
| site_id | AC9 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GUA B 622 |
| Chain | Residue |
| B | TYR416 |
| B | HIS437 |
| B | ARG481 |
| B | ARG492 |
| B | PTE623 |
| B | TYR307 |
| B | GLU308 |
| site_id | B1 |
| Number of Residues | 1 |
| Details | FIRST MOLYBDOPTERIN BINDING MOTIF |
| Chain | Residue |
| B | ASP333 |
| site_id | B2 |
| Number of Residues | 1 |
| Details | SECOND MOLYBDOPTERIN BINDING MOTIF |
| Chain | Residue |
| B | GLU486 |
| site_id | BC1 |
| Number of Residues | 36 |
| Details | BINDING SITE FOR RESIDUE PTE B 623 |
| Chain | Residue |
| B | LYS75 |
| B | GLY91 |
| B | ASN92 |
| B | LEU93 |
| B | GLY94 |
| B | GLY179 |
| B | ARG180 |
| B | ALA181 |
| B | ALA182 |
| B | GLY183 |
| B | ARG184 |
| B | ASP306 |
| 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 | CA620 |
| B | SF4621 |
| B | GUA622 |
| B | HOH624 |
| B | HOH629 |
| B | HOH630 |
| B | HOH666 |
| B | HOH667 |
| B | HOH668 |
| B | HOH669 |
| site_id | BC2 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE SF4 C 621 |
| Chain | Residue |
| C | SER72 |
| C | LYS75 |
| C | GLY283 |
| C | CYS284 |
| C | CYS287 |
| C | MET289 |
| C | PRO290 |
| C | CYS291 |
| C | CYS491 |
| C | PTE623 |
| site_id | BC3 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE GUA C 622 |
| Chain | Residue |
| C | TYR307 |
| C | GLU308 |
| C | TYR416 |
| C | HIS437 |
| C | ARG481 |
| C | ARG492 |
| C | LEU493 |
| C | VAL496 |
| C | GLU497 |
| C | PTE623 |
| site_id | BC4 |
| Number of Residues | 36 |
| Details | BINDING SITE FOR RESIDUE PTE C 623 |
| 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 | ASP306 |
| C | GLU308 |
| C | ASN309 |
| C | ALA332 |
| C | ASP333 |
| C | MET337 |
| C | ASP338 |
| C | THR339 |
| C | ILE340 |
| C | HIS436 |
| C | HIS437 |
| C | LYS438 |
| C | PHE485 |
| C | GLU486 |
| C | ALA490 |
| C | CYS491 |
| C | ARG492 |
| C | CA620 |
| C | SF4621 |
| C | GUA622 |
| C | HOH657 |
| C | HOH666 |
| C | HOH669 |
| C | HOH670 |
| C | HOH672 |
| site_id | BC5 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SF4 D 621 |
| Chain | Residue |
| D | ARG180 |
| D | GLY283 |
| D | CYS284 |
| D | CYS287 |
| D | MET289 |
| D | CYS291 |
| D | CYS491 |
| D | PTE623 |
| site_id | BC6 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE GUA D 622 |
| Chain | Residue |
| D | TYR307 |
| D | GLU308 |
| D | TYR416 |
| D | HIS437 |
| D | TRP441 |
| D | ARG481 |
| D | ARG492 |
| D | LEU493 |
| D | VAL496 |
| D | GLU497 |
| D | PTE623 |
| site_id | BC7 |
| Number of Residues | 37 |
| Details | BINDING SITE FOR RESIDUE PTE D 623 |
| 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 | ASP306 |
| D | GLU308 |
| D | ASN309 |
| D | ALA332 |
| D | ASP333 |
| D | MET337 |
| D | ASP338 |
| D | THR339 |
| D | ILE340 |
| D | HIS436 |
| D | HIS437 |
| D | LYS438 |
| D | PHE485 |
| D | GLU486 |
| D | ALA490 |
| D | CYS491 |
| D | ARG492 |
| D | CA620 |
| D | SF4621 |
| D | GUA622 |
| D | HOH634 |
| D | HOH642 |
| D | HOH671 |
| D | HOH672 |
| D | HOH673 |
| D | HOH674 |
| site_id | C1 |
| Number of Residues | 1 |
| Details | FIRST MOLYBDOPTERIN BINDING MOTIF |
| Chain | Residue |
| C | ASP333 |
| site_id | C2 |
| Number of Residues | 1 |
| Details | SECOND MOLYBDOPTERIN BINDING MOTIF |
| Chain | Residue |
| C | GLU486 |
| site_id | D1 |
| Number of Residues | 1 |
| Details | FIRST MOLYBDOPTERIN BINDING MOTIF |
| Chain | Residue |
| D | ASP333 |
| site_id | D2 |
| Number of Residues | 1 |
| Details | SECOND MOLYBDOPTERIN BINDING MOTIF |
| Chain | Residue |
| D | GLU486 |
