2D4E
Crystal Structure of the HpcC from Thermus Thermophilus HB8
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
| A | 0018480 | molecular_function | 5-carboxymethyl-2-hydroxymuconic-semialdehyde dehydrogenase activity |
| A | 1901023 | biological_process | 4-hydroxyphenylacetate catabolic process |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
| B | 0018480 | molecular_function | 5-carboxymethyl-2-hydroxymuconic-semialdehyde dehydrogenase activity |
| B | 1901023 | biological_process | 4-hydroxyphenylacetate catabolic process |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
| C | 0018480 | molecular_function | 5-carboxymethyl-2-hydroxymuconic-semialdehyde dehydrogenase activity |
| C | 1901023 | biological_process | 4-hydroxyphenylacetate catabolic process |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
| D | 0018480 | molecular_function | 5-carboxymethyl-2-hydroxymuconic-semialdehyde dehydrogenase activity |
| D | 1901023 | biological_process | 4-hydroxyphenylacetate catabolic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NA A 1901 |
| Chain | Residue |
| A | SER46 |
| A | LEU47 |
| A | ASP113 |
| A | TRP200 |
| A | HOH1932 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NA B 1902 |
| Chain | Residue |
| B | HOH1907 |
| B | SER46 |
| B | LEU47 |
| B | ASP113 |
| B | TRP200 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NA C 1903 |
| Chain | Residue |
| C | SER46 |
| C | LEU47 |
| C | ASP113 |
| C | TRP200 |
| C | HOH1912 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NA D 1904 |
| Chain | Residue |
| D | SER46 |
| D | LEU47 |
| D | ASP113 |
| D | TRP200 |
| D | HOH1976 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE NA C 1905 |
| Chain | Residue |
| C | GLU250 |
| C | NAD1701 |
| site_id | AC6 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE NA D 1906 |
| Chain | Residue |
| D | GLU250 |
| D | NAD1702 |
| site_id | AC7 |
| Number of Residues | 32 |
| Details | BINDING SITE FOR RESIDUE NAD C 1701 |
| Chain | Residue |
| C | ILE169 |
| C | THR170 |
| C | PRO171 |
| C | TRP172 |
| C | LEU178 |
| C | LYS196 |
| C | PRO197 |
| C | ALA198 |
| C | GLU199 |
| C | GLY229 |
| C | GLY233 |
| C | ALA234 |
| C | THR248 |
| C | GLY249 |
| C | GLU250 |
| C | THR253 |
| C | ILE256 |
| C | GLU271 |
| C | LEU272 |
| C | GLY273 |
| C | CYS305 |
| C | GLU409 |
| C | PHE411 |
| C | PHE475 |
| C | NA1905 |
| C | HOH1929 |
| C | HOH2011 |
| C | HOH2016 |
| C | HOH2110 |
| C | HOH2120 |
| C | HOH2151 |
| C | HOH2173 |
| site_id | AC8 |
| Number of Residues | 31 |
| Details | BINDING SITE FOR RESIDUE NAD D 1702 |
| Chain | Residue |
| D | ILE169 |
| D | THR170 |
| D | PRO171 |
| D | TRP172 |
| D | LEU178 |
| D | LYS196 |
| D | PRO197 |
| D | ALA198 |
| D | GLU199 |
| D | GLY229 |
| D | GLY233 |
| D | ALA234 |
| D | THR248 |
| D | GLY249 |
| D | GLU250 |
| D | THR253 |
| D | ILE256 |
| D | GLU271 |
| D | LEU272 |
| D | GLY273 |
| D | CYS305 |
| D | GLU409 |
| D | PHE411 |
| D | PHE475 |
| D | NA1906 |
| D | HOH1924 |
| D | HOH1961 |
| D | HOH2123 |
| D | HOH2131 |
| D | HOH2138 |
| D | HOH2167 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL A 1801 |
| Chain | Residue |
| A | ILE169 |
| A | GLY229 |
| A | GLY233 |
| A | THR253 |
| A | HOH1907 |
| A | HOH2017 |
| site_id | BC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL B 1802 |
| Chain | Residue |
| B | GLY229 |
| B | GLY233 |
| B | THR253 |
| B | HOH1910 |
| B | HOH1943 |
| site_id | BC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL C 1803 |
| Chain | Residue |
| C | PRO26 |
| C | LEU28 |
| C | PHE35 |
| C | THR206 |
| C | GLU210 |
| C | ARG25 |
Functional Information from PROSITE/UniProt
| site_id | PS00070 |
| Number of Residues | 12 |
| Details | ALDEHYDE_DEHYDR_CYS Aldehyde dehydrogenases cysteine active site. FsFNGERCTASS |
| Chain | Residue | Details |
| A | PHE298-SER309 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1a4s |
| Chain | Residue | Details |
| A | CYS305 | |
| A | ASN173 | |
| A | GLU271 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1a4s |
| Chain | Residue | Details |
| B | CYS305 | |
| B | ASN173 | |
| B | GLU271 |
| site_id | CSA3 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1a4s |
| Chain | Residue | Details |
| C | CYS305 | |
| C | ASN173 | |
| C | GLU271 |
| site_id | CSA4 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1a4s |
| Chain | Residue | Details |
| D | CYS305 | |
| D | ASN173 | |
| D | GLU271 |
