Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0003952 | molecular_function | NAD+ synthase (glutamine-hydrolyzing) activity |
| A | 0004359 | molecular_function | glutaminase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0008795 | molecular_function | NAD+ synthase activity |
| A | 0009435 | biological_process | NAD biosynthetic process |
| A | 0016874 | molecular_function | ligase activity |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0003952 | molecular_function | NAD+ synthase (glutamine-hydrolyzing) activity |
| B | 0004359 | molecular_function | glutaminase activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0008795 | molecular_function | NAD+ synthase activity |
| B | 0009435 | biological_process | NAD biosynthetic process |
| B | 0016874 | molecular_function | ligase activity |
| B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE MG B 308 |
| Chain | Residue |
| B | SER183 |
| B | ATP304 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG A 309 |
| Chain | Residue |
| A | SER183 |
| A | ATP303 |
| A | HOH334 |
| A | HOH381 |
| site_id | AC3 |
| Number of Residues | 33 |
| Details | BINDING SITE FOR RESIDUE DND A 301 |
| Chain | Residue |
| A | TYR142 |
| A | GLY143 |
| A | THR144 |
| A | LEU145 |
| A | ASP148 |
| A | ALA184 |
| A | LEU186 |
| A | GLN190 |
| A | PHE246 |
| A | LYS247 |
| A | ATP303 |
| A | HOH318 |
| A | HOH320 |
| A | HOH329 |
| A | HOH346 |
| A | HOH347 |
| A | HOH362 |
| A | HOH371 |
| A | HOH383 |
| A | HOH390 |
| A | HOH392 |
| A | HOH400 |
| B | ARG23 |
| B | PHE25 |
| B | TYR119 |
| B | SER122 |
| B | LEU123 |
| B | LEU128 |
| B | ALA152 |
| B | HOH357 |
| A | THR104 |
| A | ASN108 |
| A | ARG112 |
| site_id | AC4 |
| Number of Residues | 34 |
| Details | BINDING SITE FOR RESIDUE DND B 302 |
| Chain | Residue |
| A | ARG23 |
| A | PHE25 |
| A | TYR119 |
| A | SER122 |
| A | LEU123 |
| A | LEU128 |
| A | ALA152 |
| A | HOH312 |
| A | HOH405 |
| B | THR104 |
| B | ASN108 |
| B | ARG112 |
| B | TYR142 |
| B | GLY143 |
| B | THR144 |
| B | LEU145 |
| B | ASP148 |
| B | ALA184 |
| B | LEU186 |
| B | GLN190 |
| B | ASP195 |
| B | PHE246 |
| B | LYS247 |
| B | ATP304 |
| B | HOH318 |
| B | HOH319 |
| B | HOH343 |
| B | HOH369 |
| B | HOH373 |
| B | HOH381 |
| B | HOH383 |
| B | HOH395 |
| B | HOH420 |
| B | HOH429 |
| site_id | AC5 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE ATP A 303 |
| Chain | Residue |
| A | GLY31 |
| A | LEU32 |
| A | SER33 |
| A | GLY35 |
| A | LEU36 |
| A | ASP37 |
| A | SER38 |
| A | LEU56 |
| A | MET58 |
| A | ARG114 |
| A | THR132 |
| A | GLU137 |
| A | LYS161 |
| A | PRO182 |
| A | SER183 |
| A | DND301 |
| A | MG309 |
| A | HOH324 |
| A | HOH338 |
| A | HOH376 |
| A | HOH383 |
| A | HOH413 |
| A | HOH423 |
| site_id | AC6 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE ATP B 304 |
| Chain | Residue |
| B | GLY35 |
| B | LEU36 |
| B | ASP37 |
| B | SER38 |
| B | LEU56 |
| B | MET58 |
| B | ARG114 |
| B | THR132 |
| B | GLU137 |
| B | LYS161 |
| B | PRO182 |
| B | SER183 |
| B | DND302 |
| B | MG308 |
| B | HOH316 |
| B | HOH343 |
| B | HOH349 |
| B | HOH370 |
| B | HOH407 |
| B | GLY31 |
| B | LEU32 |
| B | SER33 |
Functional Information from SwissProt/UniProt
| Chain | Residue | Details |
| A | GLY31 | |
| A | THR132 | |
| A | LYS161 | |
| B | GLY31 | |
| B | THR132 | |
| B | LYS161 | |
| Chain | Residue | Details |
| A | ASP37 | |
| A | ARG112 | |
| A | GLU137 | |
| A | SER183 | |
| B | ASP37 | |
| B | ARG112 | |
| B | GLU137 | |
| B | SER183 | |
