5EKS
Structure of 3-dehydroquinate synthase from Acinetobacter baumannii in complex with NAD
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000166 | molecular_function | nucleotide binding |
A | 0003856 | molecular_function | 3-dehydroquinate synthase activity |
A | 0005737 | cellular_component | cytoplasm |
A | 0008652 | biological_process | amino acid biosynthetic process |
A | 0009073 | biological_process | aromatic amino acid family biosynthetic process |
A | 0009423 | biological_process | chorismate biosynthetic process |
A | 0016829 | molecular_function | lyase activity |
A | 0016838 | molecular_function | carbon-oxygen lyase activity, acting on phosphates |
A | 0046872 | molecular_function | metal ion binding |
B | 0000166 | molecular_function | nucleotide binding |
B | 0003856 | molecular_function | 3-dehydroquinate synthase activity |
B | 0005737 | cellular_component | cytoplasm |
B | 0008652 | biological_process | amino acid biosynthetic process |
B | 0009073 | biological_process | aromatic amino acid family biosynthetic process |
B | 0009423 | biological_process | chorismate biosynthetic process |
B | 0016829 | molecular_function | lyase activity |
B | 0016838 | molecular_function | carbon-oxygen lyase activity, acting on phosphates |
B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 34 |
Details | binding site for residue NAD A 400 |
Chain | Residue |
A | ASN41 |
A | VAL105 |
A | ASP108 |
A | THR128 |
A | THR129 |
A | LEU131 |
A | ASP135 |
A | SER136 |
A | LYS141 |
A | ASN151 |
A | GLN168 |
A | THR43 |
A | THR171 |
A | LEU172 |
A | GLU176 |
A | HOH508 |
A | HOH518 |
A | HOH530 |
A | HOH536 |
A | HOH545 |
A | HOH556 |
A | HOH591 |
A | VAL44 |
A | HOH600 |
A | HOH656 |
A | HOH662 |
A | HOH666 |
A | HOH676 |
A | TYR48 |
A | ASP70 |
A | GLU72 |
A | LYS75 |
A | GLY103 |
A | GLY104 |
site_id | AC2 |
Number of Residues | 5 |
Details | binding site for residue MG A 401 |
Chain | Residue |
A | GLU183 |
A | HIS246 |
A | HIS263 |
A | HOH610 |
A | HOH631 |
site_id | AC3 |
Number of Residues | 33 |
Details | binding site for residue NAD B 400 |
Chain | Residue |
B | ASN41 |
B | THR43 |
B | VAL44 |
B | TYR48 |
B | ASP70 |
B | GLU72 |
B | LYS75 |
B | GLY103 |
B | GLY104 |
B | VAL105 |
B | ASP108 |
B | THR128 |
B | THR129 |
B | LEU131 |
B | ASP135 |
B | LYS141 |
B | ASN151 |
B | GLN168 |
B | THR171 |
B | LEU172 |
B | GLU176 |
B | HOH527 |
B | HOH536 |
B | HOH549 |
B | HOH562 |
B | HOH573 |
B | HOH583 |
B | HOH595 |
B | HOH597 |
B | HOH598 |
B | HOH687 |
B | HOH690 |
B | HOH751 |
site_id | AC4 |
Number of Residues | 6 |
Details | binding site for residue MG B 401 |
Chain | Residue |
B | GLU183 |
B | HIS246 |
B | HIS263 |
B | HOH520 |
B | HOH648 |
B | HOH788 |