5B47
2-Oxoacid:Ferredoxin Oxidoreductase 2 from Sulfolobus tokodai - pyruvate complex
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003824 | molecular_function | catalytic activity |
A | 0006086 | biological_process | acetyl-CoA biosynthetic process from pyruvate |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0016903 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors |
A | 0018491 | molecular_function | 2-oxobutyrate synthase activity |
A | 0019164 | molecular_function | pyruvate synthase activity |
A | 0047553 | molecular_function | 2-oxoglutarate synthase activity |
B | 0000287 | molecular_function | magnesium ion binding |
B | 0003824 | molecular_function | catalytic activity |
B | 0006086 | biological_process | acetyl-CoA biosynthetic process from pyruvate |
B | 0016491 | molecular_function | oxidoreductase activity |
B | 0018491 | molecular_function | 2-oxobutyrate synthase activity |
B | 0019164 | molecular_function | pyruvate synthase activity |
B | 0030976 | molecular_function | thiamine pyrophosphate binding |
B | 0046872 | molecular_function | metal ion binding |
B | 0047553 | molecular_function | 2-oxoglutarate synthase activity |
B | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | binding site for residue PYR A 701 |
Chain | Residue |
A | SER42 |
A | THR257 |
A | ARG344 |
A | PRO352 |
B | ILE44 |
B | TPP402 |
site_id | AC2 |
Number of Residues | 5 |
Details | binding site for residue SF4 B 401 |
Chain | Residue |
B | CYS46 |
B | CYS197 |
A | ILE44 |
B | CYS12 |
B | CYS15 |
site_id | AC3 |
Number of Residues | 22 |
Details | binding site for residue TPP B 402 |
Chain | Residue |
A | TYR254 |
A | PRO255 |
A | ILE256 |
A | GLU294 |
A | PRO318 |
A | LEU322 |
A | GLU325 |
A | PYR701 |
B | ILE44 |
B | GLY45 |
B | CYS46 |
B | SER47 |
B | HIS65 |
B | ASP90 |
B | GLY91 |
B | ASP92 |
B | ASN118 |
B | VAL120 |
B | TYR121 |
B | GLY122 |
B | LEU123 |
B | MG403 |
site_id | AC4 |
Number of Residues | 6 |
Details | binding site for residue MG B 403 |
Chain | Residue |
B | GLY89 |
B | ASP90 |
B | HIS116 |
B | ASN118 |
B | VAL120 |
B | TPP402 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000269|PubMed:27619895, ECO:0007744|PDB:5B46, ECO:0007744|PDB:5B47 |
Chain | Residue | Details |
B | CYS12 | |
B | CYS15 | |
B | ILE44 | |
B | CYS46 | |
B | ASP90 | |
B | ASN118 | |
B | VAL120 | |
B | CYS197 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000305|PubMed:27619895 |
Chain | Residue | Details |
B | HIS65 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:27619895, ECO:0007744|PDB:5B46 |
Chain | Residue | Details |
B | GLY91 | |
B | GLY122 |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | SITE: Plays an important role in the binding of CoA => ECO:0000250|UniProtKB:Q96Y68 |
Chain | Residue | Details |
B | LYS125 |