1EE1
CRYSTAL STRUCTURE OF NH3-DEPENDENT NAD+ SYNTHETASE FROM BACILLUS SUBTILIS COMPLEXED WITH ONE MOLECULE ATP, TWO MOLECULES DEAMIDO-NAD+ AND ONE MG2+ ION
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 | 0030435 | biological_process | sporulation resulting in formation of a cellular spore |
| 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 | 0030435 | biological_process | sporulation resulting in formation of a cellular spore |
| B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG A 5500 |
| Chain | Residue |
| A | THR208 |
| A | HOH2381 |
| A | HOH2382 |
| A | ATP5000 |
| site_id | AC2 |
| Number of Residues | 27 |
| Details | BINDING SITE FOR RESIDUE DND A 4000 |
| Chain | Residue |
| A | THR169 |
| A | LYS170 |
| A | ASP173 |
| A | ALA209 |
| A | LEU211 |
| A | GLU223 |
| A | HIS257 |
| A | LYS258 |
| A | HOH2101 |
| A | HOH2158 |
| A | HOH2206 |
| A | HOH2213 |
| A | HOH2223 |
| A | HOH2238 |
| A | HOH2284 |
| A | ATP5000 |
| B | TYR32 |
| B | THR36 |
| B | TYR144 |
| B | LEU153 |
| B | ASP177 |
| B | HOH2071 |
| A | PHE129 |
| A | ASN133 |
| A | ARG137 |
| A | PHE167 |
| A | PHE168 |
| site_id | AC3 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE DND B 3000 |
| Chain | Residue |
| A | TYR32 |
| A | THR36 |
| A | TYR144 |
| A | LEU153 |
| A | ASP177 |
| A | HOH2027 |
| B | PHE129 |
| B | ASN133 |
| B | ARG137 |
| B | PHE167 |
| B | PHE168 |
| B | THR169 |
| B | LYS170 |
| B | ASP173 |
| B | HIS257 |
| B | LYS258 |
| B | HOH2127 |
| B | HOH2228 |
| B | HOH2270 |
| B | HOH2304 |
| B | HOH2372 |
| B | HOH2377 |
| site_id | AC4 |
| Number of Residues | 28 |
| Details | BINDING SITE FOR RESIDUE ATP A 5000 |
| Chain | Residue |
| A | LEU43 |
| A | GLY44 |
| A | ILE45 |
| A | SER46 |
| A | GLY48 |
| A | ASP50 |
| A | SER51 |
| A | ARG78 |
| A | LEU79 |
| A | GLN84 |
| A | ARG139 |
| A | THR157 |
| A | ASP173 |
| A | LYS186 |
| A | PRO207 |
| A | THR208 |
| A | HOH2012 |
| A | HOH2019 |
| A | HOH2023 |
| A | HOH2062 |
| A | HOH2080 |
| A | HOH2238 |
| A | HOH2284 |
| A | HOH2326 |
| A | HOH2381 |
| A | HOH2382 |
| A | DND4000 |
| A | MG5500 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0007744|PDB:1EE1, ECO:0007744|PDB:1IFX, ECO:0007744|PDB:1KQP, ECO:0007744|PDB:2NSY |
| Chain | Residue | Details |
| A | TYR32 | |
| B | TYR32 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00193, ECO:0007744|PDB:1EE1, ECO:0007744|PDB:1FYD, ECO:0007744|PDB:1IH8, ECO:0007744|PDB:1KQP, ECO:0007744|PDB:1NSY, ECO:0007744|PDB:2NSY |
| Chain | Residue | Details |
| A | GLY44 | |
| A | LYS186 | |
| B | GLY44 | |
| B | LYS186 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00193, ECO:0007744|PDB:1KQP, ECO:0007744|PDB:1NSY, ECO:0007744|PDB:2NSY |
| Chain | Residue | Details |
| A | ASP50 | |
| A | GLU162 | |
| B | ASP50 | |
| B | GLU162 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0007744|PDB:1EE1, ECO:0007744|PDB:1FYD, ECO:0007744|PDB:1IH8, ECO:0007744|PDB:1KQP, ECO:0007744|PDB:1NSY, ECO:0007744|PDB:2NSY |
| Chain | Residue | Details |
| A | ARG78 | |
| A | GLN84 | |
| B | ARG78 | |
| B | GLN84 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 6 |
| Details | BINDING: in other chain => ECO:0000255|HAMAP-Rule:MF_00193, ECO:0007744|PDB:1EE1, ECO:0007744|PDB:1IFX, ECO:0007744|PDB:1KQP, ECO:0007744|PDB:2NSY |
| Chain | Residue | Details |
| A | ARG137 | |
| A | LYS170 | |
| A | HIS257 | |
| B | ARG137 | |
| B | LYS170 | |
| B | HIS257 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00193, ECO:0007744|PDB:1EE1, ECO:0007744|PDB:1KQP, ECO:0007744|PDB:1NSY, ECO:0007744|PDB:2NSY |
| Chain | Residue | Details |
| A | THR157 | |
| B | THR157 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00193, ECO:0007744|PDB:1EE1, ECO:0007744|PDB:1IFX, ECO:0007744|PDB:1KQP, ECO:0007744|PDB:2NSY |
| Chain | Residue | Details |
| A | ASP177 | |
| B | ASP177 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00193, ECO:0007744|PDB:1EE1, ECO:0007744|PDB:1FYD, ECO:0007744|PDB:1IH8, ECO:0007744|PDB:1NSY, ECO:0007744|PDB:2NSY |
| Chain | Residue | Details |
| A | THR208 | |
| B | THR208 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 2 |
| Details | BINDING: in other chain => ECO:0007744|PDB:1EE1, ECO:0007744|PDB:1KQP, ECO:0007744|PDB:2NSY |
| Chain | Residue | Details |
| A | GLU223 | |
| B | GLU223 |
