3NX3
Crystal structure of acetylornithine aminotransferase (argD) from Campylobacter jejuni
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003992 | molecular_function | N2-acetyl-L-ornithine:2-oxoglutarate 5-aminotransferase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006525 | biological_process | arginine metabolic process |
| A | 0006526 | biological_process | arginine biosynthetic process |
| A | 0008483 | molecular_function | transaminase activity |
| A | 0030170 | molecular_function | pyridoxal phosphate binding |
| A | 0042802 | molecular_function | identical protein binding |
| B | 0003992 | molecular_function | N2-acetyl-L-ornithine:2-oxoglutarate 5-aminotransferase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006525 | biological_process | arginine metabolic process |
| B | 0006526 | biological_process | arginine biosynthetic process |
| B | 0008483 | molecular_function | transaminase activity |
| B | 0030170 | molecular_function | pyridoxal phosphate binding |
| B | 0042802 | molecular_function | identical protein binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG A 396 |
| Chain | Residue |
| A | HOH457 |
| A | HOH541 |
| A | HOH565 |
| A | HOH597 |
| A | HOH655 |
| A | HOH826 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MG A 397 |
| Chain | Residue |
| A | LYS378 |
| A | HOH400 |
| A | HOH457 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MG A 398 |
| Chain | Residue |
| A | ASN198 |
| A | PHE201 |
| A | HOH747 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG A 399 |
| Chain | Residue |
| A | ILE320 |
| A | PHE323 |
| A | ASP324 |
| A | CYS326 |
| A | HOH656 |
| A | HOH814 |
Functional Information from PROSITE/UniProt
| site_id | PS00600 |
| Number of Residues | 37 |
| Details | AA_TRANSFER_CLASS_3 Aminotransferases class-III pyridoxal-phosphate attachment site. LIaDEIqc.GMgRsGkffayehaqilp....DIMtsAKal.GC |
| Chain | Residue | Details |
| A | LEU216-CYS252 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01107 |
| Chain | Residue | Details |
| A | GLY102 | |
| B | ASP219 | |
| B | SER277 | |
| B | THR278 | |
| A | PHE134 | |
| A | ARG137 | |
| A | ASP219 | |
| A | SER277 | |
| A | THR278 | |
| B | GLY102 | |
| B | PHE134 | |
| B | ARG137 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | MOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000255|HAMAP-Rule:MF_01107 |
| Chain | Residue | Details |
| A | LYS248 | |
| B | LYS248 |
