6C8Q
Crystal structure of NAD synthetase (NadE) from Enterococcus faecalis in complex with NAD+
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 |
| 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 |
| C | 0003952 | molecular_function | NAD+ synthase (glutamine-hydrolyzing) activity |
| C | 0004359 | molecular_function | glutaminase activity |
| C | 0005524 | molecular_function | ATP binding |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0008795 | molecular_function | NAD+ synthase activity |
| C | 0009435 | biological_process | NAD+ biosynthetic process |
| D | 0003952 | molecular_function | NAD+ synthase (glutamine-hydrolyzing) activity |
| D | 0004359 | molecular_function | glutaminase activity |
| D | 0005524 | molecular_function | ATP binding |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0008795 | molecular_function | NAD+ synthase activity |
| D | 0009435 | biological_process | NAD+ biosynthetic process |
| E | 0003952 | molecular_function | NAD+ synthase (glutamine-hydrolyzing) activity |
| E | 0004359 | molecular_function | glutaminase activity |
| E | 0005524 | molecular_function | ATP binding |
| E | 0005737 | cellular_component | cytoplasm |
| E | 0008795 | molecular_function | NAD+ synthase activity |
| E | 0009435 | biological_process | NAD+ biosynthetic process |
| F | 0003952 | molecular_function | NAD+ synthase (glutamine-hydrolyzing) activity |
| F | 0004359 | molecular_function | glutaminase activity |
| F | 0005524 | molecular_function | ATP binding |
| F | 0005737 | cellular_component | cytoplasm |
| F | 0008795 | molecular_function | NAD+ synthase activity |
| F | 0009435 | biological_process | NAD+ biosynthetic process |
| G | 0003952 | molecular_function | NAD+ synthase (glutamine-hydrolyzing) activity |
| G | 0004359 | molecular_function | glutaminase activity |
| G | 0005524 | molecular_function | ATP binding |
| G | 0005737 | cellular_component | cytoplasm |
| G | 0008795 | molecular_function | NAD+ synthase activity |
| G | 0009435 | biological_process | NAD+ biosynthetic process |
| H | 0003952 | molecular_function | NAD+ synthase (glutamine-hydrolyzing) activity |
| H | 0004359 | molecular_function | glutaminase activity |
| H | 0005524 | molecular_function | ATP binding |
| H | 0005737 | cellular_component | cytoplasm |
| H | 0008795 | molecular_function | NAD+ synthase activity |
| H | 0009435 | biological_process | NAD+ biosynthetic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 21 |
| Details | binding site for residue NAD A 301 |
| Chain | Residue |
| A | PHE133 |
| A | LYS262 |
| A | HOH402 |
| A | HOH455 |
| A | HOH490 |
| B | TYR34 |
| B | HIS38 |
| B | PHE40 |
| B | TYR148 |
| B | GLY156 |
| B | ASP181 |
| A | ASN137 |
| C | VAL226 |
| C | GLY229 |
| A | ARG141 |
| A | PHE171 |
| A | PHE172 |
| A | THR173 |
| A | LYS174 |
| A | ALA227 |
| A | HIS261 |
| site_id | AC2 |
| Number of Residues | 18 |
| Details | binding site for residue NAD B 301 |
| Chain | Residue |
| A | TYR34 |
| A | HIS38 |
| A | PHE40 |
| A | TYR148 |
| A | GLY156 |
| A | ASP181 |
| B | PHE133 |
| B | ASN137 |
| B | ARG141 |
| B | ALA170 |
| B | PHE171 |
| B | PHE172 |
| B | THR173 |
| B | LYS174 |
| B | ALA227 |
| B | HIS261 |
| B | LYS262 |
| B | HOH472 |
| site_id | AC3 |
| Number of Residues | 21 |
| Details | binding site for residue NAD C 301 |
| Chain | Residue |
| A | VAL226 |
| A | GLY229 |
| C | PHE133 |
| C | ASN137 |
| C | ARG141 |
| C | ALA170 |
| C | PHE171 |
| C | PHE172 |
| C | THR173 |
| C | LYS174 |
| C | ALA227 |
| C | HIS261 |
| C | LYS262 |
| C | HOH401 |
| C | HOH411 |
| G | TYR34 |
| G | HIS38 |
| G | PHE40 |
| G | TYR148 |
| G | GLY156 |
| G | ASP181 |
| site_id | AC4 |
| Number of Residues | 15 |
| Details | binding site for residue NAD D 301 |
| Chain | Residue |
| D | PHE133 |
| D | ASN137 |
| D | ARG141 |
| D | PHE171 |
| D | PHE172 |
| D | LYS174 |
| D | HIS261 |
| D | LYS262 |
| D | HOH419 |
| D | HOH462 |
| F | TYR34 |
| F | HIS38 |
| F | PHE40 |
| F | GLY156 |
| F | ASP181 |
| site_id | AC5 |
| Number of Residues | 16 |
| Details | binding site for residue NAD E 301 |
| Chain | Residue |
| E | PHE133 |
| E | ASN137 |
| E | ARG141 |
| E | PHE171 |
| E | PHE172 |
| E | THR173 |
| E | LYS174 |
| E | HIS261 |
| E | LYS262 |
| E | HOH415 |
| H | TYR34 |
| H | HIS38 |
| H | PHE40 |
| H | GLY156 |
| H | ALA157 |
| H | ASP181 |
| site_id | AC6 |
| Number of Residues | 16 |
| Details | binding site for residue NAD F 301 |
| Chain | Residue |
| F | ASN137 |
| F | ARG141 |
| F | PHE171 |
| F | PHE172 |
| F | THR173 |
| F | LYS174 |
| F | HIS261 |
| F | LYS262 |
| D | TYR34 |
| D | HIS38 |
| D | LEU41 |
| D | TYR148 |
| D | GLY156 |
| D | ASP181 |
| F | PHE133 |
| F | GLY136 |
| site_id | AC7 |
| Number of Residues | 20 |
| Details | binding site for residue NAD G 301 |
| Chain | Residue |
| C | TYR34 |
| C | HIS38 |
| C | PHE40 |
| C | TYR148 |
| C | GLY156 |
| C | ASP181 |
| G | PHE133 |
| G | ASN137 |
| G | ARG141 |
| G | GLU166 |
| G | PHE171 |
| G | PHE172 |
| G | THR173 |
| G | LYS174 |
| G | ASP177 |
| G | ASP224 |
| G | HIS261 |
| G | LYS262 |
| G | HOH407 |
| G | HOH457 |
| site_id | AC8 |
| Number of Residues | 17 |
| Details | binding site for residue NAD H 301 |
| Chain | Residue |
| E | TYR34 |
| E | HIS38 |
| E | PHE40 |
| E | TYR148 |
| E | GLY156 |
| E | ASP181 |
| H | PHE133 |
| H | ASN137 |
| H | ARG141 |
| H | PHE171 |
| H | PHE172 |
| H | THR173 |
| H | LYS174 |
| H | HIS261 |
| H | LYS262 |
| H | HOH435 |
| H | HOH459 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 120 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00193","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |






