3D2P
Crystal structure of N-acetylglutamate synthase from Neisseria gonorrhoeae complexed with coenzyme A and L-arginine
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004042 | molecular_function | L-glutamate N-acetyltransferase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006526 | biological_process | L-arginine biosynthetic process |
| A | 0008652 | biological_process | amino acid biosynthetic process |
| A | 0016740 | molecular_function | transferase activity |
| A | 0016746 | molecular_function | acyltransferase activity |
| A | 0016747 | molecular_function | acyltransferase activity, transferring groups other than amino-acyl groups |
| A | 0140085 | molecular_function | L-amino-acid N-acetyltransferase activity |
| B | 0004042 | molecular_function | L-glutamate N-acetyltransferase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006526 | biological_process | L-arginine biosynthetic process |
| B | 0008652 | biological_process | amino acid biosynthetic process |
| B | 0016740 | molecular_function | transferase activity |
| B | 0016746 | molecular_function | acyltransferase activity |
| B | 0016747 | molecular_function | acyltransferase activity, transferring groups other than amino-acyl groups |
| B | 0140085 | molecular_function | L-amino-acid N-acetyltransferase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE COA A 437 |
| Chain | Residue |
| A | LEU307 |
| A | THR395 |
| A | GLU397 |
| A | TRP398 |
| A | ARG402 |
| A | LEU357 |
| A | GLN364 |
| A | ASP365 |
| A | GLY366 |
| A | GLY367 |
| A | GLY369 |
| A | GLU370 |
| A | ASN394 |
| site_id | AC2 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE COA B 437 |
| Chain | Residue |
| B | PRO214 |
| B | LEU307 |
| B | LEU357 |
| B | GLN364 |
| B | ASP365 |
| B | GLY366 |
| B | GLY367 |
| B | TYR368 |
| B | GLY369 |
| B | GLU370 |
| B | THR395 |
| B | GLU397 |
| B | TRP398 |
| B | HOH479 |
| site_id | AC3 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE ARG A 438 |
| Chain | Residue |
| A | TYR17 |
| A | LYS201 |
| A | GLU220 |
| A | GLN257 |
| A | GLU270 |
| A | LEU271 |
| A | THR273 |
| A | ASN275 |
| A | ILE277 |
| A | GLY278 |
| A | THR279 |
| A | SER280 |
| A | ASP334 |
| A | HOH449 |
| site_id | AC4 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE ARG B 438 |
| Chain | Residue |
| B | TYR17 |
| B | LYS201 |
| B | GLU220 |
| B | THR221 |
| B | GLN257 |
| B | GLU270 |
| B | LEU271 |
| B | THR273 |
| B | ASN275 |
| B | ILE277 |
| B | GLY278 |
| B | SER280 |
| B | ASP334 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ygh |
| Chain | Residue | Details |
| A | GLU353 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ygh |
| Chain | Residue | Details |
| B | GLU353 |
