6UXK
Structure of serine hydroxymethyltransferase 8 from Glycine max cultivar Forrest 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 | 5 |
| Details | binding site for residue EDO A 501 |
| Chain | Residue |
| A | GLY52 |
| A | HOH617 |
| A | HOH636 |
| B | GLY52 |
| B | HOH717 |
| site_id | AC2 |
| Number of Residues | 2 |
| Details | binding site for residue EDO B 601 |
| Chain | Residue |
| A | PHE111 |
| B | PHE111 |
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 |
