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 |