1UMD
branched-chain 2-oxo acid dehydrogenase (E1) from Thermus thermophilus HB8 with 4-methyl-2-oxopentanoate as an intermediate
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003863 | molecular_function | 3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring) activity |
A | 0005515 | molecular_function | protein binding |
A | 0009083 | biological_process | branched-chain amino acid catabolic process |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0016624 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, disulfide as acceptor |
A | 0046872 | molecular_function | metal ion binding |
B | 0003824 | molecular_function | catalytic activity |
B | 0003863 | molecular_function | 3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring) activity |
B | 0005515 | molecular_function | protein binding |
B | 0007584 | biological_process | response to nutrient |
B | 0009083 | biological_process | branched-chain amino acid catabolic process |
B | 0016491 | molecular_function | oxidoreductase activity |
C | 0003863 | molecular_function | 3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring) activity |
C | 0005515 | molecular_function | protein binding |
C | 0009083 | biological_process | branched-chain amino acid catabolic process |
C | 0016491 | molecular_function | oxidoreductase activity |
C | 0016624 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, disulfide as acceptor |
C | 0046872 | molecular_function | metal ion binding |
D | 0003824 | molecular_function | catalytic activity |
D | 0003863 | molecular_function | 3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring) activity |
D | 0005515 | molecular_function | protein binding |
D | 0007584 | biological_process | response to nutrient |
D | 0009083 | biological_process | branched-chain amino acid catabolic process |
D | 0016491 | molecular_function | oxidoreductase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG A 1401 |
Chain | Residue |
A | ASP175 |
A | ASN204 |
A | TYR206 |
A | TPP1402 |
A | HOH1435 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG C 2401 |
Chain | Residue |
C | HOH2425 |
C | ASP175 |
C | ASN204 |
C | TYR206 |
C | TPP2402 |
site_id | AC3 |
Number of Residues | 26 |
Details | BINDING SITE FOR RESIDUE TPP A 1402 |
Chain | Residue |
A | TYR94 |
A | TYR95 |
A | ARG96 |
A | SER144 |
A | PRO145 |
A | ILE146 |
A | GLY174 |
A | ASP175 |
A | GLY176 |
A | ALA177 |
A | GLU180 |
A | ASN204 |
A | TYR206 |
A | ALA207 |
A | ILE208 |
A | HIS273 |
A | MG1401 |
A | COI1403 |
A | HOH1413 |
A | HOH1434 |
A | HOH1435 |
D | GLU29 |
D | LEU58 |
D | GLU60 |
D | GLN82 |
D | TYR86 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE COI A 1403 |
Chain | Residue |
A | PHE66 |
A | SER144 |
A | TPP1402 |
D | TYR86 |
D | HIS129 |
site_id | AC5 |
Number of Residues | 26 |
Details | BINDING SITE FOR RESIDUE TPP C 2402 |
Chain | Residue |
B | GLU29 |
B | LEU58 |
B | GLU60 |
B | GLN82 |
B | TYR86 |
C | TYR94 |
C | TYR95 |
C | ARG96 |
C | SER144 |
C | PRO145 |
C | ILE146 |
C | GLY174 |
C | ASP175 |
C | GLY176 |
C | ALA177 |
C | GLU180 |
C | ASN204 |
C | TYR206 |
C | ALA207 |
C | ILE208 |
C | HIS273 |
C | MG2401 |
C | COI2403 |
C | HOH2422 |
C | HOH2425 |
C | HOH2439 |
site_id | AC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE COI C 2403 |
Chain | Residue |
B | TYR86 |
B | HIS129 |
C | PHE66 |
C | SER144 |
C | TPP2402 |
Functional Information from PROSITE/UniProt
site_id | PS00014 |
Number of Residues | 4 |
Details | ER_TARGET Endoplasmic reticulum targeting sequence. KEEL |
Chain | Residue | Details |
A | LYS364-LEU367 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: Proton acceptor => ECO:0000305 |
Chain | Residue | Details |
B | HIS129 | |
A | HIS273 | |
C | PHE66 | |
C | TYR94 | |
C | TYR95 | |
C | MET128 | |
C | SER144 | |
C | GLY174 | |
C | ASP175 | |
C | ASN204 | |
C | TYR206 | |
D | HIS129 | |
C | HIS273 | |
A | TYR95 | |
A | MET128 | |
A | SER144 | |
A | GLY174 | |
A | ASP175 | |
A | ASN204 | |
A | TYR206 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000269|PubMed:15033367 |
Chain | Residue | Details |
B | GLU29 | |
B | GLN82 | |
D | GLU29 | |
D | GLN82 |
site_id | SWS_FT_FI3 |
Number of Residues | 6 |
Details | BINDING: |
Chain | Residue | Details |
B | LEU58 | |
B | PHE83 | |
B | TYR86 | |
D | LEU58 | |
D | PHE83 | |
D | TYR86 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000305 |
Chain | Residue | Details |
B | HIS129 | |
D | HIS129 |