4ADC
Structural and functional study of succinyl-ornithine transaminase from E. coli
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003992 | molecular_function | N2-acetyl-L-ornithine:2-oxoglutarate 5-transaminase activity |
| A | 0005829 | cellular_component | cytosol |
| A | 0006520 | biological_process | amino acid metabolic process |
| A | 0006525 | biological_process | arginine metabolic process |
| A | 0006526 | biological_process | L-arginine biosynthetic process |
| A | 0006527 | biological_process | L-arginine catabolic process |
| A | 0006593 | biological_process | L-ornithine catabolic process |
| A | 0008483 | molecular_function | transaminase activity |
| A | 0030170 | molecular_function | pyridoxal phosphate binding |
| A | 0043825 | molecular_function | succinylornithine:2-oxoglutarate transaminase activity |
| B | 0003992 | molecular_function | N2-acetyl-L-ornithine:2-oxoglutarate 5-transaminase activity |
| B | 0005829 | cellular_component | cytosol |
| B | 0006520 | biological_process | amino acid metabolic process |
| B | 0006525 | biological_process | arginine metabolic process |
| B | 0006526 | biological_process | L-arginine biosynthetic process |
| B | 0006527 | biological_process | L-arginine catabolic process |
| B | 0006593 | biological_process | L-ornithine catabolic process |
| B | 0008483 | molecular_function | transaminase activity |
| B | 0030170 | molecular_function | pyridoxal phosphate binding |
| B | 0043825 | molecular_function | succinylornithine:2-oxoglutarate transaminase activity |
| C | 0003992 | molecular_function | N2-acetyl-L-ornithine:2-oxoglutarate 5-transaminase activity |
| C | 0005829 | cellular_component | cytosol |
| C | 0006520 | biological_process | amino acid metabolic process |
| C | 0006525 | biological_process | arginine metabolic process |
| C | 0006526 | biological_process | L-arginine biosynthetic process |
| C | 0006527 | biological_process | L-arginine catabolic process |
| C | 0006593 | biological_process | L-ornithine catabolic process |
| C | 0008483 | molecular_function | transaminase activity |
| C | 0030170 | molecular_function | pyridoxal phosphate binding |
| C | 0043825 | molecular_function | succinylornithine:2-oxoglutarate transaminase activity |
| D | 0003992 | molecular_function | N2-acetyl-L-ornithine:2-oxoglutarate 5-transaminase activity |
| D | 0005829 | cellular_component | cytosol |
| D | 0006520 | biological_process | amino acid metabolic process |
| D | 0006525 | biological_process | arginine metabolic process |
| D | 0006526 | biological_process | L-arginine biosynthetic process |
| D | 0006527 | biological_process | L-arginine catabolic process |
| D | 0006593 | biological_process | L-ornithine catabolic process |
| D | 0008483 | molecular_function | transaminase activity |
| D | 0030170 | molecular_function | pyridoxal phosphate binding |
| D | 0043825 | molecular_function | succinylornithine:2-oxoglutarate transaminase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE PLP A 1403 |
| Chain | Residue |
| A | SER104 |
| A | VAL225 |
| A | GLN226 |
| A | HOH2104 |
| A | HOH2126 |
| A | HOH2139 |
| A | HOH2175 |
| A | HOH2176 |
| A | HOH2177 |
| B | THR281 |
| A | GLY105 |
| A | ALA106 |
| A | PHE138 |
| A | HIS139 |
| A | GLY140 |
| A | GLU190 |
| A | GLU195 |
| A | ASP223 |
| site_id | AC2 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE PLP B 1403 |
| Chain | Residue |
| A | THR281 |
| A | HOH2082 |
| A | HOH2083 |
| A | HOH2148 |
| A | HOH2150 |
| B | SER104 |
| B | GLY105 |
| B | ALA106 |
| B | PHE138 |
| B | HIS139 |
| B | GLY140 |
| B | GLU190 |
| B | ASP223 |
| B | VAL225 |
| B | GLN226 |
| B | LYS252 |
| B | HOH2077 |
| B | HOH2095 |
| B | HOH2146 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NA B 1404 |
| Chain | Residue |
| B | ILE91 |
| B | THR94 |
| B | PHE95 |
| B | ALA96 |
| B | HOH2048 |
| B | HOH2049 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE MG B 1999 |
| Chain | Residue |
| A | HOH2114 |
| A | HOH2114 |
| A | HOH2116 |
| A | HOH2116 |
| B | LYS118 |
| B | LYS118 |
| B | HOH2059 |
| B | HOH2059 |
| site_id | AC5 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE PLP C 1403 |
| Chain | Residue |
| C | SER104 |
| C | GLY105 |
| C | ALA106 |
| C | PHE138 |
| C | HIS139 |
| C | GLY140 |
| C | GLU190 |
| C | GLU195 |
| C | ASP223 |
| C | VAL225 |
| C | GLN226 |
| C | LYS252 |
| C | HOH2080 |
| C | HOH2094 |
| C | HOH2096 |
| C | HOH2104 |
| C | HOH2125 |
| C | HOH2126 |
| C | HOH2127 |
| D | THR281 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NA C 1404 |
| Chain | Residue |
| C | ILE91 |
| C | THR94 |
| C | PHE95 |
| C | ALA96 |
| C | HOH2055 |
| C | HOH2056 |
| site_id | AC7 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE PLP D 1403 |
| Chain | Residue |
| C | THR281 |
| C | HOH2062 |
| C | HOH2063 |
| C | HOH2110 |
| D | SER104 |
| D | GLY105 |
| D | ALA106 |
| D | ASN109 |
| D | PHE138 |
| D | HIS139 |
| D | GLY140 |
| D | GLU190 |
| D | ASP223 |
| D | VAL225 |
| D | GLN226 |
| D | LYS252 |
| D | HOH2040 |
| D | HOH2046 |
| D | HOH2068 |
Functional Information from PROSITE/UniProt
| site_id | PS00600 |
| Number of Residues | 38 |
| Details | AA_TRANSFER_CLASS_3 Aminotransferases class-III pyridoxal-phosphate attachment site. LIfDEVqt.GVgRtGelyaymhygvtp....DLLttAKalgGG |
| Chain | Residue | Details |
| A | LEU220-GLY257 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
