5YB0
Crystal Structure of Wild Type Phosphoserine aminotransferase (PSAT) from E. histolytica
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004648 | molecular_function | O-phospho-L-serine:2-oxoglutarate transaminase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006564 | biological_process | L-serine biosynthetic process |
| A | 0030170 | molecular_function | pyridoxal phosphate binding |
| B | 0004648 | molecular_function | O-phospho-L-serine:2-oxoglutarate transaminase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006564 | biological_process | L-serine biosynthetic process |
| B | 0030170 | molecular_function | pyridoxal phosphate binding |
| C | 0004648 | molecular_function | O-phospho-L-serine:2-oxoglutarate transaminase activity |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0006564 | biological_process | L-serine biosynthetic process |
| C | 0030170 | molecular_function | pyridoxal phosphate binding |
| D | 0004648 | molecular_function | O-phospho-L-serine:2-oxoglutarate transaminase activity |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0006564 | biological_process | L-serine biosynthetic process |
| D | 0030170 | molecular_function | pyridoxal phosphate binding |
| E | 0004648 | molecular_function | O-phospho-L-serine:2-oxoglutarate transaminase activity |
| E | 0005737 | cellular_component | cytoplasm |
| E | 0006564 | biological_process | L-serine biosynthetic process |
| E | 0030170 | molecular_function | pyridoxal phosphate binding |
| F | 0004648 | molecular_function | O-phospho-L-serine:2-oxoglutarate transaminase activity |
| F | 0005737 | cellular_component | cytoplasm |
| F | 0006564 | biological_process | L-serine biosynthetic process |
| F | 0030170 | molecular_function | pyridoxal phosphate binding |
| G | 0004648 | molecular_function | O-phospho-L-serine:2-oxoglutarate transaminase activity |
| G | 0005737 | cellular_component | cytoplasm |
| G | 0006564 | biological_process | L-serine biosynthetic process |
| G | 0030170 | molecular_function | pyridoxal phosphate binding |
| H | 0004648 | molecular_function | O-phospho-L-serine:2-oxoglutarate transaminase activity |
| H | 0005737 | cellular_component | cytoplasm |
| H | 0006564 | biological_process | L-serine biosynthetic process |
| H | 0030170 | molecular_function | pyridoxal phosphate binding |
| I | 0004648 | molecular_function | O-phospho-L-serine:2-oxoglutarate transaminase activity |
| I | 0005737 | cellular_component | cytoplasm |
| I | 0006564 | biological_process | L-serine biosynthetic process |
| I | 0030170 | molecular_function | pyridoxal phosphate binding |
| J | 0004648 | molecular_function | O-phospho-L-serine:2-oxoglutarate transaminase activity |
| J | 0005737 | cellular_component | cytoplasm |
| J | 0006564 | biological_process | L-serine biosynthetic process |
| J | 0030170 | molecular_function | pyridoxal phosphate binding |
| K | 0004648 | molecular_function | O-phospho-L-serine:2-oxoglutarate transaminase activity |
| K | 0005737 | cellular_component | cytoplasm |
| K | 0006564 | biological_process | L-serine biosynthetic process |
| K | 0030170 | molecular_function | pyridoxal phosphate binding |
| L | 0004648 | molecular_function | O-phospho-L-serine:2-oxoglutarate transaminase activity |
| L | 0005737 | cellular_component | cytoplasm |
| L | 0006564 | biological_process | L-serine biosynthetic process |
| L | 0030170 | molecular_function | pyridoxal phosphate binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 12 |
| Details | binding site for residue PLP A 401 |
| Chain | Residue |
| A | GLY76 |
| A | LYS191 |
| B | ASN232 |
| B | THR233 |
| A | ALA77 |
| A | SER78 |
| A | TRP101 |
| A | ASN146 |
| A | THR148 |
| A | ASP167 |
| A | SER169 |
| A | GLN190 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | binding site for residue CL A 402 |
| Chain | Residue |
| A | GLY99 |
| A | VAL100 |
| A | TRP101 |
| site_id | AC3 |
| Number of Residues | 2 |
| Details | binding site for residue CL B 402 |
| Chain | Residue |
| B | VAL100 |
| B | TRP101 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | binding site for residue CL C 402 |
| Chain | Residue |
| C | VAL100 |
| C | ASN147 |
| C | THR148 |
| C | ILE149 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | binding site for residue CL D 402 |
| Chain | Residue |
| D | VAL100 |
| D | TRP101 |
| D | ILE149 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | binding site for residue CL E 402 |
| Chain | Residue |
| E | VAL100 |
| E | TRP101 |
| E | ASN147 |
| E | THR148 |
| E | ILE149 |
| site_id | AC7 |
| Number of Residues | 12 |
| Details | binding site for residue PLP H 401 |
| Chain | Residue |
| E | ASN232 |
| E | THR233 |
| H | GLY76 |
| H | ALA77 |
| H | SER78 |
| H | PHE81 |
| H | TRP101 |
| H | THR144 |
| H | THR148 |
| H | SER169 |
| H | GLN190 |
| H | LYS191 |
| site_id | AC8 |
| Number of Residues | 9 |
| Details | binding site for residue PLP K 401 |
| Chain | Residue |
| K | GLY76 |
| K | ALA77 |
| K | SER78 |
| K | TRP101 |
| K | ASN146 |
| K | THR148 |
| K | ASP167 |
| K | SER169 |
| L | THR233 |
| site_id | AC9 |
| Number of Residues | 13 |
| Details | binding site for Di-peptide PLP B 401 and LYS B 191 |
| Chain | Residue |
| A | ASN232 |
| A | THR233 |
| B | GLY76 |
| B | ALA77 |
| B | SER78 |
| B | TRP101 |
| B | THR148 |
| B | ASP167 |
| B | SER169 |
| B | ALA189 |
| B | GLN190 |
| B | ASN192 |
| B | TYR334 |
| site_id | AD1 |
| Number of Residues | 14 |
| Details | binding site for Di-peptide PLP C 401 and LYS C 191 |
| Chain | Residue |
| C | ALA11 |
| C | GLY76 |
| C | ALA77 |
| C | SER78 |
| C | TRP101 |
| C | THR144 |
| C | THR148 |
| C | ASP167 |
| C | SER169 |
| C | ALA189 |
| C | GLN190 |
| C | ASN192 |
| D | ASN232 |
| D | THR233 |
| site_id | AD2 |
| Number of Residues | 15 |
| Details | binding site for Di-peptide PLP D 401 and LYS D 191 |
| Chain | Residue |
| C | ASN232 |
| C | THR233 |
| D | GLY76 |
| D | ALA77 |
| D | SER78 |
| D | PHE81 |
| D | TRP101 |
| D | THR144 |
| D | THR148 |
| D | ASP167 |
| D | SER169 |
| D | ALA189 |
| D | GLN190 |
| D | ASN192 |
| D | TYR334 |
| site_id | AD3 |
| Number of Residues | 13 |
| Details | binding site for Di-peptide PLP E 401 and LYS E 191 |
| Chain | Residue |
| E | SER169 |
| E | ALA189 |
| E | GLN190 |
| E | ASN192 |
| E | TYR334 |
| H | THR233 |
| E | GLY76 |
| E | ALA77 |
| E | SER78 |
| E | PHE81 |
| E | TRP101 |
| E | THR144 |
| E | ASP167 |
| site_id | AD4 |
| Number of Residues | 13 |
| Details | binding site for Di-peptide PLP F 401 and LYS F 191 |
| Chain | Residue |
| F | GLY76 |
| F | ALA77 |
| F | SER78 |
| F | PHE81 |
| F | TRP101 |
| F | THR148 |
| F | ASP167 |
| F | SER169 |
| F | ALA189 |
| F | GLN190 |
| F | ASN192 |
| G | ASN232 |
| G | THR233 |
| site_id | AD5 |
| Number of Residues | 17 |
| Details | binding site for Di-peptide PLP G 401 and LYS G 191 |
| Chain | Residue |
| F | ASN232 |
| F | THR233 |
| G | GLY76 |
| G | ALA77 |
| G | SER78 |
| G | PHE81 |
| G | TRP101 |
| G | THR144 |
| G | THR148 |
| G | ASP167 |
| G | SER169 |
| G | SER170 |
| G | ALA189 |
| G | GLN190 |
| G | ASN192 |
| G | TYR334 |
| G | HOH506 |
| site_id | AD6 |
| Number of Residues | 15 |
| Details | binding site for Di-peptide PLP I 401 and LYS I 191 |
| Chain | Residue |
| I | GLY76 |
| I | ALA77 |
| I | SER78 |
| I | PHE81 |
| I | TRP101 |
| I | THR144 |
| I | THR148 |
| I | ASP167 |
| I | SER169 |
| I | ALA189 |
| I | GLN190 |
| I | ASN192 |
| I | TYR334 |
| J | ASN232 |
| J | THR233 |
| site_id | AD7 |
| Number of Residues | 15 |
| Details | binding site for Di-peptide PLP I 401 and LYS I 191 |
| Chain | Residue |
| I | GLY76 |
| I | ALA77 |
| I | SER78 |
| I | PHE81 |
| I | TRP101 |
| I | THR144 |
| I | THR148 |
| I | ASP167 |
| I | SER169 |
| I | ALA189 |
| I | GLN190 |
| I | ASN192 |
| I | TYR334 |
| J | ASN232 |
| J | THR233 |
