1BJO
THE STRUCTURE OF PHOSPHOSERINE AMINOTRANSFERASE FROM E. COLI IN COMPLEX WITH ALPHA-METHYL-L-GLUTAMATE
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 | 0008652 | biological_process | amino acid biosynthetic process |
| A | 0016740 | molecular_function | transferase activity |
| A | 0030170 | molecular_function | pyridoxal phosphate binding |
| A | 0033359 | biological_process | lysine biosynthetic process via diaminopimelate and N-succinyl-2-amino-6-ketopimelate |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0042823 | biological_process | pyridoxal phosphate biosynthetic process |
| 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 | 0008652 | biological_process | amino acid biosynthetic process |
| B | 0016740 | molecular_function | transferase activity |
| B | 0030170 | molecular_function | pyridoxal phosphate binding |
| B | 0033359 | biological_process | lysine biosynthetic process via diaminopimelate and N-succinyl-2-amino-6-ketopimelate |
| B | 0042803 | molecular_function | protein homodimerization activity |
| B | 0042823 | biological_process | pyridoxal phosphate biosynthetic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE PLP A 363 |
| Chain | Residue |
| A | GLN197 |
| A | LYS198 |
| A | GAM364 |
| B | ASN239 |
| B | THR240 |
| A | GLY75 |
| A | GLY76 |
| A | ARG77 |
| A | TRP102 |
| A | THR153 |
| A | ASP174 |
| A | SER176 |
| site_id | AC2 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE GAM A 364 |
| Chain | Residue |
| A | SER9 |
| A | GLY10 |
| A | TRP102 |
| A | THR153 |
| A | ILE154 |
| A | LYS198 |
| A | HIS328 |
| A | ARG335 |
| A | PLP363 |
| A | HOH365 |
| B | ARG42 |
| site_id | PPA |
| Number of Residues | 1 |
| Details | PLP BINDING SITE. |
| Chain | Residue |
| A | LYS198 |
| site_id | PPB |
| Number of Residues | 1 |
| Details | PLP BINDING SITE. |
| Chain | Residue |
| B | LLP198 |
Functional Information from PROSITE/UniProt
| site_id | PS00595 |
| Number of Residues | 20 |
| Details | AA_TRANSFER_CLASS_5 Aminotransferases class-V pyridoxal-phosphate attachment site. YGVIyaGAQKnigpa.GlTiV |
| Chain | Residue | Details |
| A | TYR189-VAL208 | |
| B | TYR189-VAL208 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 16 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-(pyridoxal phosphate)lysine"} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | a catalytic site defined by CSA, PubMed 10024454 |
| Chain | Residue | Details |
| A | TRP102 | |
| A | LYS198 | |
| A | ASP174 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | a catalytic site defined by CSA, PubMed 10024454 |
| Chain | Residue | Details |
| B | TRP102 | |
| B | ASP174 |
| site_id | MCSA1 |
| Number of Residues | 3 |
| Details | M-CSA 424 |
| Chain | Residue | Details |
| B | TRP102 | electrostatic stabiliser, steric role |
| B | ASP174 | electrostatic stabiliser, steric role |
| B | LLP198 | covalent catalysis, proton shuttle (general acid/base) |
