5HUL
Crystal Structure of NadC Deletion Mutant in Cubic Space Group
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004514 | molecular_function | nicotinate-nucleotide diphosphorylase (carboxylating) activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0009435 | biological_process | NAD biosynthetic process |
| A | 0016757 | molecular_function | glycosyltransferase activity |
| A | 0016763 | molecular_function | pentosyltransferase activity |
| A | 0019363 | biological_process | pyridine nucleotide biosynthetic process |
| A | 0034213 | biological_process | quinolinate catabolic process |
| B | 0004514 | molecular_function | nicotinate-nucleotide diphosphorylase (carboxylating) activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0009435 | biological_process | NAD biosynthetic process |
| B | 0016757 | molecular_function | glycosyltransferase activity |
| B | 0016763 | molecular_function | pentosyltransferase activity |
| B | 0019363 | biological_process | pyridine nucleotide biosynthetic process |
| B | 0034213 | biological_process | quinolinate catabolic process |
| C | 0004514 | molecular_function | nicotinate-nucleotide diphosphorylase (carboxylating) activity |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0009435 | biological_process | NAD biosynthetic process |
| C | 0016757 | molecular_function | glycosyltransferase activity |
| C | 0016763 | molecular_function | pentosyltransferase activity |
| C | 0019363 | biological_process | pyridine nucleotide biosynthetic process |
| C | 0034213 | biological_process | quinolinate catabolic process |
| D | 0004514 | molecular_function | nicotinate-nucleotide diphosphorylase (carboxylating) activity |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0009435 | biological_process | NAD biosynthetic process |
| D | 0016757 | molecular_function | glycosyltransferase activity |
| D | 0016763 | molecular_function | pentosyltransferase activity |
| D | 0019363 | biological_process | pyridine nucleotide biosynthetic process |
| D | 0034213 | biological_process | quinolinate catabolic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | binding site for residue PO4 A 301 |
| Chain | Residue |
| A | LYS140 |
| A | ASN248 |
| A | GLY268 |
| A | HIS272 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue PO4 A 302 |
| Chain | Residue |
| A | LYS140 |
| B | ARG105 |
| B | ASP278 |
| B | PHE279 |
| B | SER280 |
| site_id | AC3 |
| Number of Residues | 1 |
| Details | binding site for residue PO4 A 303 |
| Chain | Residue |
| A | ARG242 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | binding site for residue PO4 A 304 |
| Chain | Residue |
| A | THR138 |
| A | ARG139 |
| A | HIS161 |
| A | ARG162 |
| A | MET170 |
| A | LYS172 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | binding site for residue PO4 A 305 |
| Chain | Residue |
| A | ARG105 |
| A | PHE279 |
| B | LYS140 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | binding site for residue PO4 B 301 |
| Chain | Residue |
| B | LYS140 |
| B | ASN248 |
| B | GLY268 |
| B | SER269 |
| B | HIS272 |
| site_id | AC7 |
| Number of Residues | 1 |
| Details | binding site for residue PO4 B 302 |
| Chain | Residue |
| B | ARG242 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | binding site for residue PO4 B 303 |
| Chain | Residue |
| A | ASN144 |
| B | THR16 |
| B | ALA19 |
| B | ASN144 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | binding site for residue PO4 B 304 |
| Chain | Residue |
| B | ARG139 |
| B | HIS161 |
| B | ARG162 |
| B | MET170 |
| B | LYS172 |
| B | GLU202 |
| site_id | AD1 |
| Number of Residues | 3 |
| Details | binding site for residue PO4 B 305 |
| Chain | Residue |
| B | HIS76 |
| D | LEU284 |
| D | THR285 |
| site_id | AD2 |
| Number of Residues | 6 |
| Details | binding site for residue PO4 C 301 |
| Chain | Residue |
| C | ASN248 |
| C | ILE249 |
| C | SER267 |
| C | GLY268 |
| C | SER269 |
| C | HIS272 |
| site_id | AD3 |
| Number of Residues | 1 |
| Details | binding site for residue PO4 C 302 |
| Chain | Residue |
| C | ARG242 |
| site_id | AD4 |
| Number of Residues | 4 |
| Details | binding site for residue PO4 C 303 |
| Chain | Residue |
| C | ARG139 |
| C | ARG162 |
| C | MET170 |
| C | LYS172 |
| site_id | AD5 |
| Number of Residues | 1 |
| Details | binding site for residue PO4 C 304 |
| Chain | Residue |
| C | ARG258 |
| site_id | AD6 |
| Number of Residues | 5 |
| Details | binding site for residue PO4 D 301 |
| Chain | Residue |
| D | LYS140 |
| D | ASN248 |
| D | GLY268 |
| D | SER269 |
| D | HIS272 |
| site_id | AD7 |
| Number of Residues | 1 |
| Details | binding site for residue PO4 D 302 |
| Chain | Residue |
| D | ARG242 |
| site_id | AD8 |
| Number of Residues | 5 |
| Details | binding site for residue PO4 D 303 |
| Chain | Residue |
| D | THR138 |
| D | ARG139 |
| D | ARG162 |
| D | MET170 |
| D | LYS172 |
| site_id | AD9 |
| Number of Residues | 3 |
| Details | binding site for residue PO4 D 304 |
| Chain | Residue |
| B | PHE47 |
| D | LYS49 |
| D | SER280 |
| site_id | AE1 |
| Number of Residues | 3 |
| Details | binding site for residue PO4 D 305 |
| Chain | Residue |
| C | LYS140 |
| D | LYS49 |
| D | PHE279 |
