5HUP
Crystal Structure of NadC from Streptococcus pyogenes
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004514 | molecular_function | nicotinate-nucleotide diphosphorylase (carboxylating) activity |
| A | 0009435 | biological_process | NAD+ biosynthetic process |
| A | 0016763 | molecular_function | pentosyltransferase activity |
| B | 0004514 | molecular_function | nicotinate-nucleotide diphosphorylase (carboxylating) activity |
| B | 0009435 | biological_process | NAD+ biosynthetic process |
| B | 0016763 | molecular_function | pentosyltransferase activity |
| C | 0004514 | molecular_function | nicotinate-nucleotide diphosphorylase (carboxylating) activity |
| C | 0009435 | biological_process | NAD+ biosynthetic process |
| C | 0016763 | molecular_function | pentosyltransferase activity |
| E | 0004514 | molecular_function | nicotinate-nucleotide diphosphorylase (carboxylating) activity |
| E | 0009435 | biological_process | NAD+ biosynthetic process |
| E | 0016763 | molecular_function | pentosyltransferase activity |
| F | 0004514 | molecular_function | nicotinate-nucleotide diphosphorylase (carboxylating) activity |
| F | 0009435 | biological_process | NAD+ biosynthetic process |
| F | 0016763 | molecular_function | pentosyltransferase activity |
| H | 0004514 | molecular_function | nicotinate-nucleotide diphosphorylase (carboxylating) activity |
| H | 0009435 | biological_process | NAD+ biosynthetic process |
| H | 0016763 | molecular_function | pentosyltransferase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 1 |
| Details | binding site for residue SO4 A 301 |
| Chain | Residue |
| A | ARG243 |
| site_id | AC2 |
| Number of Residues | 2 |
| Details | binding site for residue SO4 A 302 |
| Chain | Residue |
| A | ARG243 |
| E | ARG191 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 A 303 |
| Chain | Residue |
| A | LYS141 |
| A | GLY269 |
| A | SER270 |
| site_id | AC4 |
| Number of Residues | 2 |
| Details | binding site for residue SO4 A 304 |
| Chain | Residue |
| A | ARG140 |
| A | ARG163 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 B 301 |
| Chain | Residue |
| B | ARG140 |
| B | ARG163 |
| B | MET171 |
| B | THR139 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 B 302 |
| Chain | Residue |
| B | LYS141 |
| B | GLY269 |
| B | SER270 |
| B | HIS273 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 C 301 |
| Chain | Residue |
| C | ARG106 |
| E | LYS141 |
| E | LYS173 |
| site_id | AC8 |
| Number of Residues | 2 |
| Details | binding site for residue SO4 C 302 |
| Chain | Residue |
| C | SER281 |
| C | LYS283 |
| site_id | AC9 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 C 303 |
| Chain | Residue |
| C | SER268 |
| C | GLY269 |
| C | SER270 |
| site_id | AD1 |
| Number of Residues | 5 |
| Details | binding site for residue SO4 E 301 |
| Chain | Residue |
| E | THR139 |
| E | ARG140 |
| E | HIS162 |
| E | ARG163 |
| E | MET171 |
| site_id | AD2 |
| Number of Residues | 2 |
| Details | binding site for residue SO4 E 302 |
| Chain | Residue |
| E | LYS141 |
| E | GLY269 |
| site_id | AD3 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 F 301 |
| Chain | Residue |
| F | THR139 |
| F | ARG140 |
| F | ARG163 |
| site_id | AD4 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 F 302 |
| Chain | Residue |
| F | LYS141 |
| F | GLY269 |
| F | SER270 |
| site_id | AD5 |
| Number of Residues | 2 |
| Details | binding site for residue SO4 H 301 |
| Chain | Residue |
| H | ARG140 |
| H | ARG163 |
| site_id | AD6 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 H 302 |
| Chain | Residue |
| H | LYS141 |
| H | GLY269 |
| H | HIS273 |
| site_id | AD7 |
| Number of Residues | 1 |
| Details | binding site for residue SO4 H 303 |
| Chain | Residue |
| H | ARG106 |
