4RKC
Psychrophilic aromatic amino acids aminotransferase from Psychrobacter sp. B6
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003824 | molecular_function | catalytic activity |
A | 0004838 | molecular_function | L-tyrosine:2-oxoglutarate aminotransferase 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 | 0033585 | biological_process | L-phenylalanine biosynthetic process from chorismate via phenylpyruvate |
A | 0042802 | molecular_function | identical protein binding |
A | 0046872 | molecular_function | metal ion binding |
B | 0003824 | molecular_function | catalytic activity |
B | 0004838 | molecular_function | L-tyrosine:2-oxoglutarate aminotransferase 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 | 0033585 | biological_process | L-phenylalanine biosynthetic process from chorismate via phenylpyruvate |
B | 0042802 | molecular_function | identical protein binding |
B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG A 401 |
Chain | Residue |
A | HOH770 |
A | HOH779 |
A | HOH780 |
A | HOH781 |
A | HOH782 |
A | HOH869 |
site_id | AC2 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE NO3 A 402 |
Chain | Residue |
A | TRP130 |
A | ASN183 |
A | TYR214 |
A | PHE348 |
A | ARG374 |
A | PMP409 |
A | HOH811 |
A | ILE13 |
A | ILE33 |
A | GLY34 |
site_id | AC3 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE NO3 A 403 |
Chain | Residue |
A | MET1 |
A | PHE2 |
A | GLU3 |
A | ARG4 |
A | ILE5 |
A | HOH540 |
B | PHE118 |
site_id | AC4 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE NO3 A 404 |
Chain | Residue |
A | LEU81 |
A | MET221 |
A | HIS304 |
A | VAL308 |
A | HOH751 |
A | HOH804 |
A | HOH834 |
site_id | AC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE NO3 A 405 |
Chain | Residue |
A | GLU39 |
A | ARG317 |
A | MET321 |
A | ASN381 |
A | SER382 |
site_id | AC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE NO3 A 406 |
Chain | Residue |
A | SER277 |
A | ARG280 |
A | ARG281 |
A | HOH853 |
B | TYR8 |
B | ALA135 |
site_id | AC7 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE NO3 A 407 |
Chain | Residue |
A | THR342 |
A | ALA343 |
A | ASN345 |
site_id | AC8 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE NO3 A 408 |
Chain | Residue |
A | PRO72 |
A | GLY73 |
A | LYS76 |
site_id | AC9 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE PMP A 409 |
Chain | Residue |
A | GLY102 |
A | GLY103 |
A | SER104 |
A | TRP130 |
A | ASN183 |
A | ASP211 |
A | TYR214 |
A | SER243 |
A | SER245 |
A | LYS246 |
A | ARG254 |
A | NO3402 |
A | HOH811 |
B | TYR65 |
site_id | BC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG B 401 |
Chain | Residue |
A | HOH526 |
A | HOH527 |
B | HOH542 |
B | HOH543 |
B | HOH544 |
B | HOH592 |
site_id | BC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE NO3 B 402 |
Chain | Residue |
B | GLY34 |
B | TRP130 |
B | ASN183 |
B | ARG374 |
site_id | BC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE NO3 B 403 |
Chain | Residue |
B | LEU81 |
B | MET221 |
B | HIS304 |
B | HOH771 |
site_id | BC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE NO3 B 404 |
Chain | Residue |
B | LYS319 |
B | ARG322 |
B | THR323 |
B | THR342 |
B | HOH633 |
site_id | BC5 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE PMP B 405 |
Chain | Residue |
A | TYR65 |
B | GLY102 |
B | GLY103 |
B | SER104 |
B | TRP130 |
B | ASN183 |
B | ASP211 |
B | ALA213 |
B | TYR214 |
B | SER243 |
B | SER245 |
B | LYS246 |
B | ARG254 |
B | HOH591 |
B | HOH870 |
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 |