2VUN
The Crystal Structure of Enamidase at 1.9 A Resolution - A new Member of the Amidohydrolase Superfamily
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0016810 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds |
| A | 0043792 | molecular_function | enamidase activity |
| A | 0046872 | molecular_function | metal ion binding |
| A | 1901848 | biological_process | nicotinate catabolic process |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0016810 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds |
| B | 0043792 | molecular_function | enamidase activity |
| B | 0046872 | molecular_function | metal ion binding |
| B | 1901848 | biological_process | nicotinate catabolic process |
| C | 0016787 | molecular_function | hydrolase activity |
| C | 0016810 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds |
| C | 0043792 | molecular_function | enamidase activity |
| C | 0046872 | molecular_function | metal ion binding |
| C | 1901848 | biological_process | nicotinate catabolic process |
| D | 0016787 | molecular_function | hydrolase activity |
| D | 0016810 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds |
| D | 0043792 | molecular_function | enamidase activity |
| D | 0046872 | molecular_function | metal ion binding |
| D | 1901848 | biological_process | nicotinate catabolic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE ZN A 401 |
| Chain | Residue |
| A | HIS67 |
| A | HIS69 |
| A | GLU164 |
| A | ASP276 |
| A | FE402 |
| A | CL501 |
| A | HOH2362 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE FE A 402 |
| Chain | Residue |
| A | HIS220 |
| A | ZN401 |
| A | HOH2205 |
| A | HOH2222 |
| A | HOH2362 |
| A | GLU164 |
| A | HIS193 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL A 501 |
| Chain | Residue |
| A | ZN401 |
| A | HOH2205 |
| A | HOH2362 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE ZN B 401 |
| Chain | Residue |
| B | HIS67 |
| B | HIS69 |
| B | GLU164 |
| B | ASP276 |
| B | FE402 |
| B | CL501 |
| B | HOH2314 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE FE B 402 |
| Chain | Residue |
| B | GLU164 |
| B | HIS193 |
| B | HIS220 |
| B | ZN401 |
| B | HOH2173 |
| B | HOH2188 |
| B | HOH2314 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL B 501 |
| Chain | Residue |
| B | ZN401 |
| B | HOH2173 |
| B | HOH2227 |
| B | HOH2314 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ZN C 401 |
| Chain | Residue |
| C | HIS67 |
| C | HIS69 |
| C | GLU164 |
| C | ASP276 |
| C | CL501 |
| C | HOH2312 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FE C 402 |
| Chain | Residue |
| C | GLU164 |
| C | HIS193 |
| C | HIS220 |
| C | HOH2177 |
| C | HOH2186 |
| C | HOH2312 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CL C 501 |
| Chain | Residue |
| C | ZN401 |
| C | HOH2177 |
| C | HOH2186 |
| C | HOH2215 |
| C | HOH2312 |
| site_id | BC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE ZN D 401 |
| Chain | Residue |
| D | HIS67 |
| D | HIS69 |
| D | GLU164 |
| D | ASP276 |
| D | FE402 |
| D | CL501 |
| D | HOH2246 |
| site_id | BC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE FE D 402 |
| Chain | Residue |
| D | GLU164 |
| D | HIS193 |
| D | HIS220 |
| D | ZN401 |
| D | HOH2139 |
| D | HOH2149 |
| D | HOH2246 |
| site_id | BC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CL D 501 |
| Chain | Residue |
| D | HIS69 |
| D | ZN401 |
| D | HOH2139 |
| D | HOH2150 |
| D | HOH2246 |
| site_id | BC4 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL D1390 |
| Chain | Residue |
| D | GLY100 |
| D | SER101 |
| D | ARG107 |
| D | PRO108 |
| D | THR114 |
| D | LEU117 |
| D | ALA139 |
| D | VAL140 |
| D | ILE141 |
| site_id | BC5 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE GOL C1390 |
| Chain | Residue |
| C | GLY100 |
| C | SER101 |
| C | ARG107 |
| C | PRO108 |
| C | THR114 |
| C | LEU117 |
| C | ALA139 |
| C | VAL140 |
| C | ILE141 |
| C | HOH2139 |
| site_id | BC6 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL B1390 |
| Chain | Residue |
| B | GLY100 |
| B | SER101 |
| B | ARG107 |
| B | PRO108 |
| B | THR114 |
| B | LEU117 |
| B | ALA139 |
| B | VAL140 |
| B | ILE141 |
| site_id | BC7 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL A1390 |
| Chain | Residue |
| A | SER101 |
| A | ARG107 |
| A | PRO108 |
| A | THR114 |
| A | LEU117 |
| A | ALA139 |
| A | VAL140 |
| A | ILE141 |
| A | HOH2156 |
| site_id | BC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL A1391 |
| Chain | Residue |
| A | GLY266 |
| A | GLN267 |
| A | LEU268 |
| A | GLY269 |
| A | ARG270 |
| A | HOH2363 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 24 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:18805424 |
| Chain | Residue | Details |
| A | HIS67 | |
| B | HIS193 | |
| B | HIS220 | |
| B | ASP276 | |
| C | HIS67 | |
| C | HIS69 | |
| C | GLU164 | |
| C | HIS193 | |
| C | HIS220 | |
| C | ASP276 | |
| D | HIS67 | |
| A | HIS69 | |
| D | HIS69 | |
| D | GLU164 | |
| D | HIS193 | |
| D | HIS220 | |
| D | ASP276 | |
| A | GLU164 | |
| A | HIS193 | |
| A | HIS220 | |
| A | ASP276 | |
| B | HIS67 | |
| B | HIS69 | |
| B | GLU164 |
