4MSO
X-ray crystal structure of a serine hydroxymethyl transferase in apo form from Burkholderia cenocepacia
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004372 | molecular_function | glycine hydroxymethyltransferase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0006545 | biological_process | glycine biosynthetic process |
| A | 0006730 | biological_process | one-carbon metabolic process |
| A | 0008652 | biological_process | amino acid biosynthetic process |
| A | 0016740 | molecular_function | transferase activity |
| A | 0019264 | biological_process | glycine biosynthetic process from serine |
| A | 0030170 | molecular_function | pyridoxal phosphate binding |
| A | 0035999 | biological_process | tetrahydrofolate interconversion |
| A | 0046653 | biological_process | tetrahydrofolate metabolic process |
| B | 0004372 | molecular_function | glycine hydroxymethyltransferase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0006545 | biological_process | glycine biosynthetic process |
| B | 0006730 | biological_process | one-carbon metabolic process |
| B | 0008652 | biological_process | amino acid biosynthetic process |
| B | 0016740 | molecular_function | transferase activity |
| B | 0019264 | biological_process | glycine biosynthetic process from serine |
| B | 0030170 | molecular_function | pyridoxal phosphate binding |
| B | 0035999 | biological_process | tetrahydrofolate interconversion |
| B | 0046653 | biological_process | tetrahydrofolate metabolic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE PO4 A 501 |
| Chain | Residue |
| A | GLY99 |
| B | HOH886 |
| A | SER100 |
| A | THR227 |
| A | HIS229 |
| A | LYS230 |
| A | HOH748 |
| A | HOH858 |
| B | GLY260 |
| B | GLY261 |
| site_id | AC2 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE PO4 A 502 |
| Chain | Residue |
| A | SER137 |
| A | LYS139 |
| A | HOH669 |
| A | HOH765 |
| A | HOH883 |
| B | SER252 |
| B | ALA253 |
| B | ILE254 |
| B | PHE255 |
| B | ILE258 |
| B | HOH686 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE EDO B 501 |
| Chain | Residue |
| B | PRO42 |
| B | THR369 |
| B | ARG370 |
| B | VAL413 |
| B | TYR414 |
| B | HOH729 |
| B | HOH751 |
| B | HOH829 |
| site_id | AC4 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE PO4 B 502 |
| Chain | Residue |
| A | GLY260 |
| A | GLY261 |
| A | HOH636 |
| B | SER98 |
| B | GLY99 |
| B | SER100 |
| B | THR227 |
| B | HIS229 |
| B | LYS230 |
| B | HOH674 |
| B | HOH711 |
| B | HOH961 |
Functional Information from PROSITE/UniProt
| site_id | PS00096 |
| Number of Residues | 17 |
| Details | SHMT Serine hydroxymethyltransferase pyridoxal-phosphate attachment site. DFvTTTTHKSLrGPRGG |
| Chain | Residue | Details |
| A | ASP222-GLY238 |
