5VIU
Crystal Structure of Acetylornithine Aminotransferase from Elizabethkingia anophelis
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004587 | molecular_function | ornithine aminotransferase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0008483 | molecular_function | transaminase activity |
| A | 0010121 | biological_process | arginine catabolic process to proline via ornithine |
| A | 0019544 | biological_process | arginine catabolic process to glutamate |
| A | 0030170 | molecular_function | pyridoxal phosphate binding |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0055129 | biological_process | L-proline biosynthetic process |
| B | 0004587 | molecular_function | ornithine aminotransferase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0008483 | molecular_function | transaminase activity |
| B | 0010121 | biological_process | arginine catabolic process to proline via ornithine |
| B | 0019544 | biological_process | arginine catabolic process to glutamate |
| B | 0030170 | molecular_function | pyridoxal phosphate binding |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0055129 | biological_process | L-proline biosynthetic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 3 |
| Details | binding site for residue EDO A 501 |
| Chain | Residue |
| A | LYS44 |
| A | GLY373 |
| A | HOH707 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | binding site for residue EDO A 502 |
| Chain | Residue |
| B | ALA76 |
| B | LEU77 |
| A | HIS59 |
| A | SER60 |
| A | GLY265 |
| A | MET267 |
| A | HOH652 |
| A | HOH837 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | binding site for residue EDO A 503 |
| Chain | Residue |
| A | VAL207 |
| A | ARG343 |
| A | ILE383 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | binding site for residue EDO A 504 |
| Chain | Residue |
| A | ASN142 |
| A | ASN143 |
| A | PHE144 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | binding site for residue EDO A 505 |
| Chain | Residue |
| A | ASN226 |
| A | LEU228 |
| A | HOH637 |
| A | HOH684 |
| A | HOH868 |
| A | HOH879 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | binding site for residue EDO A 506 |
| Chain | Residue |
| A | ILE179 |
| A | GLU183 |
| A | GLN217 |
| A | HOH603 |
| site_id | AC7 |
| Number of Residues | 13 |
| Details | binding site for residue CIT A 507 |
| Chain | Residue |
| A | ASN107 |
| A | GLU111 |
| A | SER290 |
| A | THR291 |
| A | PHE292 |
| A | HOH607 |
| A | HOH612 |
| A | HOH689 |
| A | HOH759 |
| B | SER108 |
| B | GLY109 |
| B | LYS261 |
| B | PRO269 |
| site_id | AC8 |
| Number of Residues | 10 |
| Details | binding site for residue CIT A 508 |
| Chain | Residue |
| A | GLU141 |
| A | ASN142 |
| A | ASN143 |
| A | HIS145 |
| A | ASP232 |
| A | HOH675 |
| A | HOH681 |
| A | HOH810 |
| A | HOH874 |
| B | HIS288 |
| site_id | AC9 |
| Number of Residues | 10 |
| Details | binding site for residue CIT A 509 |
| Chain | Residue |
| A | LYS243 |
| A | LEU244 |
| A | HIS248 |
| A | GLN310 |
| A | SER315 |
| A | GLU316 |
| A | HOH660 |
| A | HOH726 |
| A | HOH768 |
| A | HOH890 |
| site_id | AD1 |
| Number of Residues | 5 |
| Details | binding site for residue EDO B 501 |
| Chain | Residue |
| B | LYS44 |
| B | GLY373 |
| B | HOH680 |
| B | HOH737 |
| B | HOH778 |
Functional Information from PROSITE/UniProt
| site_id | PS00600 |
| Number of Residues | 38 |
| Details | AA_TRANSFER_CLASS_3 Aminotransferases class-III pyridoxal-phosphate attachment site. FIaDEVqt.GIaRtGkliachhedvqp....DILilGKalsGG |
| Chain | Residue | Details |
| A | PHE229-GLY266 |
