5KHA
Structure of glutamine-dependent NAD+ synthetase from Acinetobacter baumannii in complex with adenosine diphosphate (ADP)
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 |
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 |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 19 |
Details | binding site for residue ADP A 600 |
Chain | Residue |
A | TYR274 |
A | HOH759 |
A | HOH777 |
A | HOH911 |
A | HOH927 |
A | HOH937 |
B | ASN369 |
B | ARG373 |
B | CYS404 |
B | THR405 |
B | LEU406 |
A | PHE280 |
A | MET380 |
A | SER383 |
A | ASN384 |
A | TYR509 |
A | LYS510 |
A | HOH734 |
A | HOH755 |
site_id | AC2 |
Number of Residues | 7 |
Details | binding site for residue EDO A 601 |
Chain | Residue |
A | GLY49 |
A | TYR50 |
A | PRO51 |
A | ALA52 |
A | GLU53 |
A | LEU56 |
A | HOH832 |
site_id | AC3 |
Number of Residues | 2 |
Details | binding site for residue CL A 602 |
Chain | Residue |
A | SER173 |
A | LYS179 |
site_id | AC4 |
Number of Residues | 18 |
Details | binding site for residue ADP B 600 |
Chain | Residue |
A | ASN369 |
A | ARG373 |
A | CYS404 |
A | THR405 |
A | LEU406 |
B | TYR274 |
B | PHE280 |
B | MET380 |
B | SER383 |
B | ASN384 |
B | GLY413 |
B | TYR509 |
B | LYS510 |
B | HOH708 |
B | HOH726 |
B | HOH825 |
B | HOH838 |
B | HOH845 |
site_id | AC5 |
Number of Residues | 7 |
Details | binding site for residue EDO B 601 |
Chain | Residue |
B | GLY49 |
B | TYR50 |
B | PRO51 |
B | ALA52 |
B | GLU53 |
B | LEU56 |
B | HOH876 |
site_id | AC6 |
Number of Residues | 2 |
Details | binding site for residue CL B 602 |
Chain | Residue |
B | SER173 |
B | LYS179 |