6N2O
2-oxoglutarate:ferredoxin oxidoreductase from Magnetococcus marinus with 2-oxoglutarate, coenzyme A and succinyl-CoA bound
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003824 | molecular_function | catalytic activity |
A | 0006979 | biological_process | response to oxidative stress |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0016903 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors |
B | 0003824 | molecular_function | catalytic activity |
B | 0016491 | molecular_function | oxidoreductase activity |
B | 0030976 | molecular_function | thiamine pyrophosphate binding |
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 | 0003824 | molecular_function | catalytic activity |
C | 0006979 | biological_process | response to oxidative stress |
C | 0016491 | molecular_function | oxidoreductase activity |
C | 0016903 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors |
D | 0003824 | molecular_function | catalytic activity |
D | 0016491 | molecular_function | oxidoreductase activity |
D | 0030976 | molecular_function | thiamine pyrophosphate binding |
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 | AC1 |
Number of Residues | 8 |
Details | binding site for residue AKG A 601 |
Chain | Residue |
A | ILE226 |
A | THR227 |
A | ARG303 |
B | ARG63 |
B | LEU135 |
B | THR136 |
B | TPP402 |
C | LEU426 |
site_id | AC2 |
Number of Residues | 11 |
Details | binding site for residue COA A 602 |
Chain | Residue |
A | GLY17 |
A | ILE18 |
A | ILE19 |
A | SER20 |
A | ARG129 |
A | ASN132 |
A | MET133 |
A | LYS157 |
B | LYS137 |
B | TYR151 |
A | GLY15 |
site_id | AC3 |
Number of Residues | 8 |
Details | binding site for residue SF4 B 401 |
Chain | Residue |
B | TRP25 |
B | CYS26 |
B | CYS29 |
B | CYS60 |
B | ASN130 |
B | CYS209 |
B | THR211 |
B | PHE212 |
site_id | AC4 |
Number of Residues | 22 |
Details | binding site for residue TPP B 402 |
Chain | Residue |
A | TYR224 |
A | PRO225 |
A | ILE226 |
A | GLU253 |
A | AKG601 |
B | HIS31 |
B | ILE58 |
B | CYS60 |
B | SER61 |
B | HIS77 |
B | ASP102 |
B | GLY103 |
B | ASP104 |
B | ASN130 |
B | ILE132 |
B | TYR133 |
B | GLY134 |
B | LEU135 |
B | THR136 |
B | MG403 |
B | HOH504 |
C | GLU284 |
site_id | AC5 |
Number of Residues | 5 |
Details | binding site for residue MG B 403 |
Chain | Residue |
B | ASP102 |
B | ASN130 |
B | ILE132 |
B | TPP402 |
B | HOH504 |
site_id | AC6 |
Number of Residues | 9 |
Details | binding site for residue SF4 D 401 |
Chain | Residue |
C | ILE46 |
D | TRP25 |
D | CYS26 |
D | CYS29 |
D | CYS60 |
D | CYS209 |
D | PRO210 |
D | THR211 |
D | PHE212 |
site_id | AC7 |
Number of Residues | 5 |
Details | binding site for residue MG D 403 |
Chain | Residue |
D | ASP102 |
D | ASN130 |
D | ILE132 |
D | TPP402 |
D | HOH502 |
site_id | AC8 |
Number of Residues | 50 |
Details | binding site for residues SCA C 601 and TPP D 402 |
Chain | Residue |
D | HIS31 |
D | ILE58 |
D | GLY59 |
D | CYS60 |
D | SER61 |
D | ARG63 |
D | HIS77 |
D | GLY101 |
D | ASP102 |
D | GLY103 |
D | ASP104 |
D | ASN130 |
D | ILE132 |
D | GLY134 |
D | LEU135 |
D | THR136 |
D | LYS137 |
D | MG403 |
D | HOH502 |
A | GLU284 |
A | LEU426 |
C | GLY15 |
C | GLU16 |
C | GLY17 |
C | ILE18 |
C | ILE19 |
C | SER20 |
C | PHE42 |
C | PRO43 |
C | ALA44 |
C | GLU45 |
C | ILE46 |
C | ARG129 |
C | ASN132 |
C | LYS157 |
C | PHE158 |
C | LYS161 |
C | ASN169 |
C | PRO225 |
C | ILE226 |
C | THR227 |
C | GLU253 |
C | ARG303 |
C | LYS399 |
C | ARG400 |
C | TYR401 |
C | LEU403 |
C | THR404 |
C | SER409 |
C | GLU430 |