4ADD
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 410 |
| Chain | Residue |
| A | SER104 |
| A | LYS252 |
| A | SUO411 |
| A | HOH2070 |
| A | HOH2095 |
| A | HOH2115 |
| A | HOH2116 |
| A | HOH2117 |
| B | THR281 |
| A | GLY105 |
| A | ALA106 |
| A | PHE138 |
| A | HIS139 |
| A | GLU190 |
| A | ASP223 |
| A | VAL225 |
| A | GLN226 |
| site_id | AC2 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE SUO A 411 |
| Chain | Residue |
| A | TYR18 |
| A | PHE138 |
| A | ARG141 |
| A | GLU195 |
| A | LYS252 |
| A | PLP410 |
| A | HOH2004 |
| A | HOH2072 |
| A | HOH2087 |
| A | HOH2115 |
| A | HOH2118 |
| B | ASN76 |
| B | GLY77 |
| B | GLY279 |
| B | THR280 |
| B | THR281 |
| site_id | AC3 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE PLP B 410 |
| Chain | Residue |
| A | THR281 |
| A | HOH2057 |
| A | HOH2099 |
| B | SER104 |
| B | GLY105 |
| B | ALA106 |
| B | PHE138 |
| B | HIS139 |
| B | GLU190 |
| B | ASP223 |
| B | VAL225 |
| B | GLN226 |
| B | LYS252 |
| B | SUO411 |
| B | HOH2048 |
| B | HOH2055 |
| B | HOH2079 |
| site_id | AC4 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE SUO B 411 |
| Chain | Residue |
| A | GLY279 |
| A | THR280 |
| A | HOH2038 |
| B | TYR18 |
| B | PHE138 |
| B | ARG141 |
| B | GLU195 |
| B | LYS252 |
| B | PLP410 |
| B | HOH2079 |
| site_id | AC5 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE PLP C 410 |
| Chain | Residue |
| C | SER104 |
| C | GLY105 |
| C | ALA106 |
| C | PHE138 |
| C | HIS139 |
| C | GLY140 |
| C | GLU190 |
| C | ASP223 |
| C | VAL225 |
| C | GLN226 |
| C | LYS252 |
| C | SUO411 |
| C | HOH2049 |
| C | HOH2054 |
| C | HOH2061 |
| C | HOH2071 |
| C | HOH2072 |
| C | HOH2073 |
| D | THR281 |
| site_id | AC6 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE SUO C 411 |
| Chain | Residue |
| C | TYR18 |
| C | PHE138 |
| C | ARG141 |
| C | GLU195 |
| C | LYS252 |
| C | PLP410 |
| C | HOH2071 |
| D | ASN76 |
| D | GLY77 |
| D | GLY279 |
| D | THR280 |
| D | THR281 |
| site_id | AC7 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE PLP D 410 |
| Chain | Residue |
| D | PHE138 |
| D | HIS139 |
| D | GLU190 |
| D | ASP223 |
| D | VAL225 |
| D | GLN226 |
| D | LYS252 |
| D | SUO411 |
| D | HOH2030 |
| D | HOH2034 |
| C | THR281 |
| C | HOH2039 |
| C | HOH2040 |
| C | HOH2066 |
| D | SER104 |
| D | GLY105 |
| D | ALA106 |
| D | ASN109 |
| site_id | AC8 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE SUO D 411 |
| Chain | Residue |
| C | GLY279 |
| C | THR280 |
| C | HOH2027 |
| D | TYR18 |
| D | PHE138 |
| D | ARG141 |
| D | GLU195 |
| D | LYS252 |
| D | PLP410 |
| D | HOH2002 |
| D | HOH2036 |
| D | HOH2050 |
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 |
