4WXG
Crystal structure of L-Serine Hydroxymethyltransferase in complex with a mixture of L-Threonine and Glycine
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004372 | molecular_function | glycine hydroxymethyltransferase activity |
| A | 0005737 | cellular_component | cytoplasm |
| 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 |
| C | 0003824 | molecular_function | catalytic activity |
| C | 0004372 | molecular_function | glycine hydroxymethyltransferase activity |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0006545 | biological_process | glycine biosynthetic process |
| C | 0006730 | biological_process | one-carbon metabolic process |
| C | 0008652 | biological_process | amino acid biosynthetic process |
| C | 0016740 | molecular_function | transferase activity |
| C | 0019264 | biological_process | glycine biosynthetic process from serine |
| C | 0030170 | molecular_function | pyridoxal phosphate binding |
| C | 0035999 | biological_process | tetrahydrofolate interconversion |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 21 |
| Details | binding site for residue 2BO A 501 |
| Chain | Residue |
| A | SER35 |
| A | THR227 |
| A | HIS229 |
| A | LYS230 |
| A | ARG363 |
| A | HOH636 |
| A | HOH681 |
| C | TYR55 |
| C | GLU57 |
| C | TYR65 |
| C | GLY261 |
| A | SER97 |
| C | GLY262 |
| C | HOH602 |
| A | GLY98 |
| A | SER99 |
| A | HIS126 |
| A | SER176 |
| A | ASP201 |
| A | ALA203 |
| A | HIS204 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | binding site for residue NA A 502 |
| Chain | Residue |
| A | PHE301 |
| A | ASN302 |
| A | HIS304 |
| A | PHE307 |
| site_id | AC3 |
| Number of Residues | 9 |
| Details | binding site for residue GOL A 503 |
| Chain | Residue |
| A | LEU154 |
| A | TYR156 |
| A | ARG180 |
| A | ASP183 |
| A | HOH664 |
| A | HOH664 |
| A | HOH683 |
| A | HOH711 |
| A | HOH752 |
| site_id | AC4 |
| Number of Residues | 21 |
| Details | binding site for residue 2BO C 501 |
| Chain | Residue |
| A | TYR55 |
| A | GLU57 |
| A | TYR65 |
| A | GLY261 |
| A | GLY262 |
| A | HOH601 |
| C | SER35 |
| C | SER97 |
| C | GLY98 |
| C | SER99 |
| C | HIS126 |
| C | SER176 |
| C | ASP201 |
| C | ALA203 |
| C | HIS204 |
| C | THR227 |
| C | HIS229 |
| C | LYS230 |
| C | ARG363 |
| C | HOH675 |
| C | HOH713 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | binding site for residue NA C 502 |
| Chain | Residue |
| C | PHE301 |
| C | ASN302 |
| C | HIS304 |
| C | PHE307 |
Functional Information from PROSITE/UniProt
| site_id | PS00096 |
| Number of Residues | 17 |
| Details | SHMT Serine hydroxymethyltransferase pyridoxal-phosphate attachment site. HVtTTTTHKTLrGPRGG |
| Chain | Residue | Details |
| A | HIS222-GLY238 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00051 |
| Chain | Residue | Details |
| A | LEU121 | |
| A | GLY125 | |
| A | SER355 | |
| C | LEU121 | |
| C | GLY125 | |
| C | SER355 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | SITE: Plays an important role in substrate specificity => ECO:0000255|HAMAP-Rule:MF_00051 |
| Chain | Residue | Details |
| A | HIS229 | |
| C | HIS229 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | MOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000255|HAMAP-Rule:MF_00051 |
| Chain | Residue | Details |
| A | LYS230 | |
| C | LYS230 |
