3NTJ
Redox regulation of Plasmodium falciparum ornithine delta-aminotransferase
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004587 | molecular_function | ornithine aminotransferase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005739 | cellular_component | mitochondrion |
| A | 0006591 | biological_process | ornithine metabolic process |
| A | 0030170 | molecular_function | pyridoxal phosphate binding |
| A | 0055129 | biological_process | L-proline biosynthetic process |
| B | 0004587 | molecular_function | ornithine aminotransferase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005739 | cellular_component | mitochondrion |
| B | 0006591 | biological_process | ornithine metabolic process |
| B | 0030170 | molecular_function | pyridoxal phosphate binding |
| B | 0055129 | biological_process | L-proline biosynthetic process |
| C | 0004587 | molecular_function | ornithine aminotransferase activity |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0005739 | cellular_component | mitochondrion |
| C | 0006591 | biological_process | ornithine metabolic process |
| C | 0030170 | molecular_function | pyridoxal phosphate binding |
| C | 0055129 | biological_process | L-proline biosynthetic process |
| D | 0004587 | molecular_function | ornithine aminotransferase activity |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0005739 | cellular_component | mitochondrion |
| D | 0006591 | biological_process | ornithine metabolic process |
| D | 0030170 | molecular_function | pyridoxal phosphate binding |
| D | 0055129 | biological_process | L-proline biosynthetic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 A 441 |
| Chain | Residue |
| A | GLY112 |
| A | ALA113 |
| A | LYS262 |
| B | SER291 |
| B | THR292 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 A 423 |
| Chain | Residue |
| A | THR292 |
| B | GLY112 |
| B | LYS262 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 C 441 |
| Chain | Residue |
| C | LYS262 |
| D | SER291 |
| D | THR292 |
| C | GLY112 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 C 423 |
| Chain | Residue |
| C | SER291 |
| C | THR292 |
| D | GLY112 |
| D | LYS262 |
Functional Information from PROSITE/UniProt
| site_id | PS00600 |
| Number of Residues | 38 |
| Details | AA_TRANSFER_CLASS_3 Aminotransferases class-III pyridoxal-phosphate attachment site. FVaDEVqt.GLgRtGkllcthhygvkp....DVIllGKalsGG |
| Chain | Residue | Details |
| A | PHE230-GLY267 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"source":"UniProtKB","id":"P04181","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
