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 | 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 | 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 | 8 |
Details | BINDING: |
Chain | Residue | Details |
B | SER9 | |
B | ARG42 | |
B | GLY76 | |
B | TRP102 | |
B | THR153 | |
B | ASP174 | |
B | GLN197 | |
B | ASN239 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | MOD_RES: N6-(pyridoxal phosphate)lysine |
Chain | Residue | Details |
B | LLP198 |
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) |