4RKD
Psychrophilic aromatic amino acids aminotransferase from Psychrobacter sp. B6 cocrystalized with aspartic acid
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004838 | molecular_function | L-tyrosine:2-oxoglutarate transaminase activity |
| A | 0005829 | cellular_component | cytosol |
| A | 0006520 | biological_process | amino acid metabolic process |
| A | 0008483 | molecular_function | transaminase activity |
| A | 0009058 | biological_process | biosynthetic process |
| A | 0030170 | molecular_function | pyridoxal phosphate binding |
| A | 0042802 | molecular_function | identical protein binding |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0004838 | molecular_function | L-tyrosine:2-oxoglutarate transaminase activity |
| B | 0005829 | cellular_component | cytosol |
| B | 0006520 | biological_process | amino acid metabolic process |
| B | 0008483 | molecular_function | transaminase activity |
| B | 0009058 | biological_process | biosynthetic process |
| B | 0030170 | molecular_function | pyridoxal phosphate binding |
| B | 0042802 | molecular_function | identical protein binding |
| C | 0003824 | molecular_function | catalytic activity |
| C | 0004838 | molecular_function | L-tyrosine:2-oxoglutarate transaminase activity |
| C | 0005829 | cellular_component | cytosol |
| C | 0006520 | biological_process | amino acid metabolic process |
| C | 0008483 | molecular_function | transaminase activity |
| C | 0009058 | biological_process | biosynthetic process |
| C | 0030170 | molecular_function | pyridoxal phosphate binding |
| C | 0042802 | molecular_function | identical protein binding |
| D | 0003824 | molecular_function | catalytic activity |
| D | 0004838 | molecular_function | L-tyrosine:2-oxoglutarate transaminase activity |
| D | 0005829 | cellular_component | cytosol |
| D | 0006520 | biological_process | amino acid metabolic process |
| D | 0008483 | molecular_function | transaminase activity |
| D | 0009058 | biological_process | biosynthetic process |
| D | 0030170 | molecular_function | pyridoxal phosphate binding |
| D | 0042802 | molecular_function | identical protein binding |
| E | 0003824 | molecular_function | catalytic activity |
| E | 0004838 | molecular_function | L-tyrosine:2-oxoglutarate transaminase activity |
| E | 0005829 | cellular_component | cytosol |
| E | 0006520 | biological_process | amino acid metabolic process |
| E | 0008483 | molecular_function | transaminase activity |
| E | 0009058 | biological_process | biosynthetic process |
| E | 0030170 | molecular_function | pyridoxal phosphate binding |
| E | 0042802 | molecular_function | identical protein binding |
| F | 0003824 | molecular_function | catalytic activity |
| F | 0004838 | molecular_function | L-tyrosine:2-oxoglutarate transaminase activity |
| F | 0005829 | cellular_component | cytosol |
| F | 0006520 | biological_process | amino acid metabolic process |
| F | 0008483 | molecular_function | transaminase activity |
| F | 0009058 | biological_process | biosynthetic process |
| F | 0030170 | molecular_function | pyridoxal phosphate binding |
| F | 0042802 | molecular_function | identical protein binding |
| G | 0003824 | molecular_function | catalytic activity |
| G | 0004838 | molecular_function | L-tyrosine:2-oxoglutarate transaminase activity |
| G | 0005829 | cellular_component | cytosol |
| G | 0006520 | biological_process | amino acid metabolic process |
| G | 0008483 | molecular_function | transaminase activity |
| G | 0009058 | biological_process | biosynthetic process |
| G | 0030170 | molecular_function | pyridoxal phosphate binding |
| G | 0042802 | molecular_function | identical protein binding |
| H | 0003824 | molecular_function | catalytic activity |
| H | 0004838 | molecular_function | L-tyrosine:2-oxoglutarate transaminase activity |
| H | 0005829 | cellular_component | cytosol |
| H | 0006520 | biological_process | amino acid metabolic process |
| H | 0008483 | molecular_function | transaminase activity |
| H | 0009058 | biological_process | biosynthetic process |
| H | 0030170 | molecular_function | pyridoxal phosphate binding |
| H | 0042802 | molecular_function | identical protein binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG A 401 |
| Chain | Residue |
| A | HOH528 |
| A | HOH530 |
| A | HOH533 |
| A | HOH594 |
| B | HOH551 |
| B | HOH552 |
| site_id | AC2 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE PLP A 402 |
| Chain | Residue |
| A | TRP130 |
| A | ASP211 |
| A | ALA213 |
| A | TYR214 |
| A | SER243 |
| A | SER245 |
| A | LYS246 |
| A | ARG254 |
| B | TYR65 |
| A | GLY102 |
| A | GLY103 |
| A | SER104 |
| site_id | AC3 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE KET A 403 |
| Chain | Residue |
| A | GLY34 |
| A | GLY102 |
| A | GLY103 |
| A | SER104 |
| A | TRP130 |
| A | ASN183 |
| A | ASP211 |
| A | TYR214 |
| A | SER243 |
| A | SER245 |
| A | LYS246 |
| A | ARG254 |
| B | TYR65 |
| B | ARG280 |
| site_id | AC4 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE PLP B 401 |
| Chain | Residue |
| A | TYR65 |
| B | GLY102 |
| B | GLY103 |
| B | SER104 |
| B | ASN183 |
| B | ASP211 |
| B | ALA213 |
| B | TYR214 |
| B | SER243 |
| B | SER245 |
| B | LYS246 |
| B | ARG254 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG C 401 |
| Chain | Residue |
| C | HOH523 |
| C | HOH569 |
| C | HOH575 |
| D | HOH542 |
| D | HOH569 |
| site_id | AC6 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE PLP C 402 |
| Chain | Residue |
| C | GLY102 |
| C | GLY103 |
| C | SER104 |
| C | TRP130 |
| C | ASN183 |
| C | ASP211 |
| C | TYR214 |
| C | SER243 |
| C | SER245 |
| C | LYS246 |
| C | ARG254 |
| C | HOH573 |
| C | HOH574 |
| D | TYR65 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE OAA C 403 |
| Chain | Residue |
| C | TYR65 |
| C | ARG280 |
| C | HOH570 |
| D | TRP130 |
| D | PMP401 |
| site_id | AC8 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE PMP D 401 |
| Chain | Residue |
| C | TYR65 |
| C | OAA403 |
| D | GLY102 |
| D | GLY103 |
| D | SER104 |
| D | TRP130 |
| D | ASN183 |
| D | ASP211 |
| D | ALA213 |
| D | TYR214 |
| D | SER243 |
| D | SER245 |
| D | LYS246 |
| D | ARG254 |
| D | HOH615 |
| site_id | AC9 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE MG E 401 |
| Chain | Residue |
| E | GLU112 |
| E | HOH523 |
| E | HOH524 |
| F | GLU112 |
| F | HOH543 |
| F | HOH545 |
| F | HOH567 |
| site_id | BC1 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE PLP E 402 |
| Chain | Residue |
| E | LYS246 |
| E | ARG254 |
| F | TYR65 |
| E | GLY102 |
| E | GLY103 |
| E | SER104 |
| E | ASN183 |
| E | ASP211 |
| E | ALA213 |
| E | TYR214 |
| E | SER243 |
| E | SER245 |
| site_id | BC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE OAA E 403 |
| Chain | Residue |
| E | GLU138 |
| E | ASP141 |
| E | ILE142 |
| E | GLU143 |
| E | HOH543 |
| E | HOH544 |
| E | HOH562 |
| site_id | BC3 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE KET E 404 |
| Chain | Residue |
| E | GLY34 |
| E | GLY102 |
| E | GLY103 |
| E | SER104 |
| E | TRP130 |
| E | ASN183 |
| E | ASP211 |
| E | TYR214 |
| E | SER243 |
| E | SER245 |
| E | LYS246 |
| E | ARG254 |
| E | HOH568 |
| F | TYR65 |
| site_id | BC4 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE PLP F 401 |
| Chain | Residue |
| E | TYR65 |
| F | GLY102 |
| F | GLY103 |
| F | SER104 |
| F | TRP130 |
| F | HIS133 |
| F | ASN183 |
| F | ASP211 |
| F | ALA213 |
| F | TYR214 |
| F | SER243 |
| F | SER245 |
| F | LYS246 |
| F | ARG254 |
| site_id | BC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG G 401 |
| Chain | Residue |
| G | HOH543 |
| G | HOH563 |
| H | HOH543 |
| H | HOH544 |
| H | HOH570 |
| H | HOH571 |
| site_id | BC6 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE KET G 402 |
| Chain | Residue |
| G | GLY102 |
| G | GLY103 |
| G | SER104 |
| G | TRP130 |
| G | ASN183 |
| G | ASP211 |
| G | TYR214 |
| G | SER243 |
| G | SER245 |
| G | LYS246 |
| G | ARG254 |
| G | ARG374 |
| H | TYR65 |
| site_id | BC7 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE PMP H 401 |
| Chain | Residue |
| G | TYR65 |
| H | GLY102 |
| H | GLY103 |
| H | SER104 |
| H | TRP130 |
| H | ASN183 |
| H | ASP211 |
| H | ALA213 |
| H | TYR214 |
| H | SER243 |
| H | SER245 |
| H | LYS246 |
| H | ARG254 |
| H | HOH574 |
Functional Information from PROSITE/UniProt
| site_id | PS00105 |
| Number of Residues | 14 |
| Details | AA_TRANSFER_CLASS_1 Aminotransferases class-I pyridoxal-phosphate attachment site. SFSKnlSLyGERVG |
| Chain | Residue | Details |
| A | SER243-GLY256 |






