3E77
Human phosphoserine aminotransferase in complex with PLP
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004648 | molecular_function | O-phospho-L-serine:2-oxoglutarate aminotransferase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0006563 | biological_process | L-serine metabolic process |
| A | 0006564 | biological_process | L-serine biosynthetic process |
| A | 0008483 | molecular_function | transaminase activity |
| A | 0008615 | biological_process | pyridoxine biosynthetic process |
| A | 0030170 | molecular_function | pyridoxal phosphate binding |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0070062 | cellular_component | extracellular exosome |
| B | 0004648 | molecular_function | O-phospho-L-serine:2-oxoglutarate aminotransferase activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0006563 | biological_process | L-serine metabolic process |
| B | 0006564 | biological_process | L-serine biosynthetic process |
| B | 0008483 | molecular_function | transaminase activity |
| B | 0008615 | biological_process | pyridoxine biosynthetic process |
| B | 0030170 | molecular_function | pyridoxal phosphate binding |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0070062 | cellular_component | extracellular exosome |
| C | 0004648 | molecular_function | O-phospho-L-serine:2-oxoglutarate aminotransferase activity |
| C | 0005515 | molecular_function | protein binding |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0005829 | cellular_component | cytosol |
| C | 0006563 | biological_process | L-serine metabolic process |
| C | 0006564 | biological_process | L-serine biosynthetic process |
| C | 0008483 | molecular_function | transaminase activity |
| C | 0008615 | biological_process | pyridoxine biosynthetic process |
| C | 0030170 | molecular_function | pyridoxal phosphate binding |
| C | 0042802 | molecular_function | identical protein binding |
| C | 0070062 | cellular_component | extracellular exosome |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE PLP A 400 |
| Chain | Residue |
| A | GLY78 |
| A | SER179 |
| A | GLN199 |
| A | LYS200 |
| A | HOH509 |
| A | HOH582 |
| B | ASN241 |
| B | THR242 |
| A | GLY79 |
| A | CYS80 |
| A | PHE83 |
| A | TRP107 |
| A | ASN154 |
| A | THR156 |
| A | ASP176 |
| A | SER178 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL A 500 |
| Chain | Residue |
| A | LEU128 |
| A | GLY129 |
| A | SER130 |
| A | LYS133 |
| site_id | AC3 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE PLP B 400 |
| Chain | Residue |
| A | ASN241 |
| A | THR242 |
| B | GLY78 |
| B | GLY79 |
| B | CYS80 |
| B | TRP107 |
| B | THR156 |
| B | ASP176 |
| B | SER178 |
| B | SER179 |
| B | GLN199 |
| B | LYS200 |
| B | HOH434 |
Functional Information from PROSITE/UniProt
| site_id | PS00595 |
| Number of Residues | 20 |
| Details | AA_TRANSFER_CLASS_5 Aminotransferases class-V pyridoxal-phosphate attachment site. FGVIfaGAQKnvgsa.GvTvV |
| Chain | Residue | Details |
| A | PHE191-VAL210 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| Details | BINDING: in other chain => ECO:0000269|PubMed:36851825, ECO:0007744|PDB:8A5W |
| Chain | Residue | Details |
| A | HIS44 | |
| A | ARG45 | |
| B | HIS44 | |
| C | ARG45 | |
| B | ARG45 | |
| C | HIS44 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 18 |
| Details | BINDING: BINDING => ECO:0000269|Ref.11, ECO:0000305|PubMed:36851825, ECO:0007744|PDB:3E77, ECO:0007744|PDB:8A5V |
| Chain | Residue | Details |
| C | THR156 | |
| C | ASP176 | |
| C | GLN199 | |
| A | GLY79 | |
| B | THR156 | |
| B | ASP176 | |
| B | GLN199 | |
| A | CYS80 | |
| A | TRP107 | |
| A | THR156 | |
| A | ASP176 | |
| A | GLN199 | |
| B | GLY79 | |
| B | CYS80 | |
| B | TRP107 | |
| C | GLY79 | |
| C | CYS80 | |
| C | TRP107 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 3 |
| Details | BINDING: in other chain => ECO:0000269|PubMed:36851825, ECO:0007744|PDB:3E77, ECO:0007744|PDB:8A5V |
| Chain | Residue | Details |
| A | ASN241 | |
| B | ASN241 | |
| C | ASN241 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 3 |
| Details | BINDING: in other chain => ECO:0000269|Ref.11, ECO:0000305|PubMed:36851825, ECO:0007744|PDB:3E77, ECO:0007744|PDB:8A5V |
| Chain | Residue | Details |
| A | THR242 | |
| B | THR242 | |
| C | THR242 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 9 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:36851825, ECO:0007744|PDB:8A5W |
| Chain | Residue | Details |
| B | HIS335 | |
| B | ARG336 | |
| B | ARG342 | |
| C | HIS335 | |
| C | ARG336 | |
| C | ARG342 | |
| A | HIS335 | |
| A | ARG336 | |
| A | ARG342 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 15 |
| Details | MOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861 |
| Chain | Residue | Details |
| A | LYS51 | |
| B | LYS333 | |
| C | LYS51 | |
| C | LYS269 | |
| C | LYS318 | |
| C | LYS323 | |
| C | LYS333 | |
| A | LYS269 | |
| A | LYS318 | |
| A | LYS323 | |
| A | LYS333 | |
| B | LYS51 | |
| B | LYS269 | |
| B | LYS318 | |
| B | LYS323 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 3 |
| Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q99K85 |
| Chain | Residue | Details |
| A | LYS127 | |
| B | LYS127 | |
| C | LYS127 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 3 |
| Details | MOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:36851825, ECO:0000269|Ref.11, ECO:0007744|PDB:3E77, ECO:0007744|PDB:8A5V |
| Chain | Residue | Details |
| A | LYS200 | |
| B | LYS200 | |
| C | LYS200 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 3 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163 |
| Chain | Residue | Details |
| A | SER331 | |
| B | SER331 | |
| C | SER331 |
