Functional Information from GO Data
Chain | GOid | namespace | contents |
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 | 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 | |