6UXH
Structure of serine hydroxymethyltransferase 8 from Glycine max cultivar Essex complexed with PLP
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004372 | molecular_function | glycine hydroxymethyltransferase activity |
A | 0019264 | biological_process | glycine biosynthetic process from serine |
A | 0030170 | molecular_function | pyridoxal phosphate binding |
A | 0035999 | biological_process | tetrahydrofolate interconversion |
B | 0004372 | molecular_function | glycine hydroxymethyltransferase activity |
B | 0019264 | biological_process | glycine biosynthetic process from serine |
B | 0030170 | molecular_function | pyridoxal phosphate binding |
B | 0035999 | biological_process | tetrahydrofolate interconversion |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | binding site for residue EDO B 501 |
Chain | Residue |
A | GLY52 |
A | HOH613 |
B | GLY52 |
B | HOH604 |
B | HOH638 |
B | HOH661 |
Functional Information from PROSITE/UniProt
site_id | PS00096 |
Number of Residues | 17 |
Details | SHMT Serine hydroxymethyltransferase pyridoxal-phosphate attachment site. DIvTTTTHKSLrGPRAG |
Chain | Residue | Details |
A | ASP236-GLY252 |