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 |