4ADB
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-aminotransferase 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 | 0042450 | biological_process | L-arginine biosynthetic process via ornithine |
| A | 0043825 | molecular_function | succinylornithine transaminase activity |
| B | 0003992 | molecular_function | N2-acetyl-L-ornithine:2-oxoglutarate 5-aminotransferase 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 | 0042450 | biological_process | L-arginine biosynthetic process via ornithine |
| B | 0043825 | molecular_function | succinylornithine transaminase activity |
| C | 0003992 | molecular_function | N2-acetyl-L-ornithine:2-oxoglutarate 5-aminotransferase 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 | 0042450 | biological_process | L-arginine biosynthetic process via ornithine |
| C | 0043825 | molecular_function | succinylornithine transaminase activity |
| D | 0003992 | molecular_function | N2-acetyl-L-ornithine:2-oxoglutarate 5-aminotransferase 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 | 0042450 | biological_process | L-arginine biosynthetic process via ornithine |
| D | 0043825 | molecular_function | succinylornithine transaminase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE PLP A 1404 |
| Chain | Residue |
| A | SER104 |
| A | LYS252 |
| A | HOH2128 |
| A | HOH2166 |
| A | HOH2168 |
| A | HOH2217 |
| A | HOH2218 |
| A | HOH2219 |
| B | THR281 |
| A | GLY105 |
| A | ALA106 |
| A | PHE138 |
| A | HIS139 |
| A | GLU190 |
| A | ASP223 |
| A | VAL225 |
| A | GLN226 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE MG A 1999 |
| Chain | Residue |
| A | HOH2110 |
| A | HOH2111 |
| A | HOH2220 |
| A | HOH2221 |
| A | HOH2222 |
| A | HOH2223 |
| C | LYS118 |
| site_id | AC3 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE PLP B 1404 |
| Chain | Residue |
| A | THR281 |
| A | HOH2101 |
| A | HOH2102 |
| A | HOH2176 |
| A | HOH2178 |
| B | SER104 |
| B | GLY105 |
| B | ALA106 |
| B | PHE138 |
| B | HIS139 |
| B | GLU190 |
| B | ASP223 |
| B | VAL225 |
| B | GLN226 |
| B | LYS252 |
| B | HOH2096 |
| B | HOH2181 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NA B 1405 |
| Chain | Residue |
| B | ILE91 |
| B | THR94 |
| B | PHE95 |
| B | ALA96 |
| B | HOH2062 |
| B | HOH2064 |
| site_id | AC5 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE MG B 1999 |
| Chain | Residue |
| A | HOH2137 |
| A | HOH2137 |
| A | HOH2138 |
| A | HOH2138 |
| B | LYS118 |
| B | LYS118 |
| B | HOH2073 |
| B | HOH2073 |
| site_id | AC6 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE PLP C 1404 |
| Chain | Residue |
| C | SER104 |
| C | GLY105 |
| C | ALA106 |
| C | PHE138 |
| C | HIS139 |
| C | GLU190 |
| C | ASP223 |
| C | VAL225 |
| C | GLN226 |
| C | LYS252 |
| C | HOH2094 |
| C | HOH2123 |
| C | HOH2153 |
| C | HOH2154 |
| C | HOH2155 |
| D | THR281 |
| site_id | AC7 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE PLP D 1404 |
| Chain | Residue |
| C | THR281 |
| C | HOH2073 |
| C | HOH2130 |
| D | SER104 |
| D | GLY105 |
| D | ALA106 |
| D | PHE138 |
| D | HIS139 |
| D | GLU190 |
| D | ASP223 |
| D | VAL225 |
| D | GLN226 |
| D | LYS252 |
| D | HOH2051 |
| D | HOH2085 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NA C 1405 |
| Chain | Residue |
| C | ILE91 |
| C | THR94 |
| C | ALA96 |
| C | HOH2063 |
| C | HOH2065 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NA A 1405 |
| Chain | Residue |
| A | ILE91 |
| A | THR94 |
| A | ALA96 |
| A | HOH2090 |
| A | HOH2093 |
| site_id | BC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE NA D 1405 |
| Chain | Residue |
| D | ALA96 |
| D | ILE91 |
| D | THR94 |
| D | PHE95 |
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 |
