3ECD
Crystal structure of serine hydroxymethyltransferase from Burkholderia pseudomallei
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| 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 |
| B | 0004372 | molecular_function | glycine hydroxymethyltransferase activity |
| B | 0005737 | cellular_component | cytoplasm |
| 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 |
| 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 |
| D | 0004372 | molecular_function | glycine hydroxymethyltransferase activity |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0006545 | biological_process | glycine biosynthetic process |
| D | 0006730 | biological_process | one-carbon metabolic process |
| D | 0008652 | biological_process | amino acid biosynthetic process |
| D | 0016740 | molecular_function | transferase activity |
| D | 0019264 | biological_process | glycine biosynthetic process from serine |
| D | 0030170 | molecular_function | pyridoxal phosphate binding |
| D | 0035999 | biological_process | tetrahydrofolate interconversion |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL A 425 |
| Chain | Residue |
| A | ARG237 |
| A | ASP286 |
| A | TYR290 |
| A | THR374 |
| A | HOH677 |
| A | HOH682 |
| D | ASN5 |
| D | PHE7 |
| site_id | AC2 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL B 425 |
| Chain | Residue |
| B | ASP286 |
| B | TYR290 |
| B | THR374 |
| B | HOH565 |
| B | HOH747 |
| B | HOH748 |
| C | ASN5 |
| C | PHE7 |
| B | ARG237 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL C 425 |
| Chain | Residue |
| B | ASN5 |
| B | PHE7 |
| C | ARG237 |
| C | ASP286 |
| C | TYR290 |
| C | THR374 |
| C | HOH888 |
| C | HOH990 |
| site_id | AC4 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL D 425 |
| Chain | Residue |
| A | ASN5 |
| A | PHE7 |
| D | ARG237 |
| D | ASP286 |
| D | TYR290 |
| D | THR374 |
| D | HOH513 |
| D | HOH543 |
| D | HOH654 |
Functional Information from PROSITE/UniProt
| site_id | PS00096 |
| Number of Residues | 17 |
| Details | SHMT Serine hydroxymethyltransferase pyridoxal-phosphate attachment site. HVvTSTTHKTLrGPRGG |
| Chain | Residue | Details |
| A | HIS226-GLY242 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00051 |
| Chain | Residue | Details |
| A | LEU125 | |
| D | LEU125 | |
| D | GLY129 | |
| D | GLU250 | |
| A | GLY129 | |
| A | GLU250 | |
| B | LEU125 | |
| B | GLY129 | |
| B | GLU250 | |
| C | LEU125 | |
| C | GLY129 | |
| C | GLU250 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | SITE: Plays an important role in substrate specificity => ECO:0000255|HAMAP-Rule:MF_00051 |
| Chain | Residue | Details |
| A | HIS233 | |
| B | HIS233 | |
| C | HIS233 | |
| D | HIS233 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | MOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000255|HAMAP-Rule:MF_00051 |
| Chain | Residue | Details |
| A | LYS234 | |
| B | LYS234 | |
| C | LYS234 | |
| D | LYS234 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1dfo |
| Chain | Residue | Details |
| A | GLU61 | |
| A | THR231 | |
| A | LYS234 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1dfo |
| Chain | Residue | Details |
| B | GLU61 | |
| B | THR231 | |
| B | LYS234 |
| site_id | CSA3 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1dfo |
| Chain | Residue | Details |
| C | GLU61 | |
| C | THR231 | |
| C | LYS234 |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1dfo |
| Chain | Residue | Details |
| D | THR231 | |
| D | LYS234 |
| site_id | CSA5 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1dfo |
| Chain | Residue | Details |
| A | HIS208 | |
| A | LYS234 |
| site_id | CSA6 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1dfo |
| Chain | Residue | Details |
| B | HIS208 | |
| B | LYS234 |
| site_id | CSA7 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1dfo |
| Chain | Residue | Details |
| C | HIS208 | |
| C | LYS234 |
| site_id | CSA8 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1dfo |
| Chain | Residue | Details |
| D | HIS208 | |
| D | LYS234 |
