6CD1
Crystal structure of Medicago truncatula serine hydroxymethyltransferase 3 (MtSHMT3), complexes with reaction intermediates
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 |
| C | 0004372 | molecular_function | glycine hydroxymethyltransferase 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 | 0019264 | biological_process | glycine biosynthetic process from serine |
| D | 0030170 | molecular_function | pyridoxal phosphate binding |
| D | 0035999 | biological_process | tetrahydrofolate interconversion |
| E | 0004372 | molecular_function | glycine hydroxymethyltransferase activity |
| E | 0019264 | biological_process | glycine biosynthetic process from serine |
| E | 0030170 | molecular_function | pyridoxal phosphate binding |
| E | 0035999 | biological_process | tetrahydrofolate interconversion |
| F | 0004372 | molecular_function | glycine hydroxymethyltransferase activity |
| F | 0019264 | biological_process | glycine biosynthetic process from serine |
| F | 0030170 | molecular_function | pyridoxal phosphate binding |
| F | 0035999 | biological_process | tetrahydrofolate interconversion |
| G | 0004372 | molecular_function | glycine hydroxymethyltransferase activity |
| G | 0019264 | biological_process | glycine biosynthetic process from serine |
| G | 0030170 | molecular_function | pyridoxal phosphate binding |
| G | 0035999 | biological_process | tetrahydrofolate interconversion |
| H | 0004372 | molecular_function | glycine hydroxymethyltransferase activity |
| H | 0019264 | biological_process | glycine biosynthetic process from serine |
| H | 0030170 | molecular_function | pyridoxal phosphate binding |
| H | 0035999 | biological_process | tetrahydrofolate interconversion |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 22 |
| Details | binding site for residue PLS A 601 |
| Chain | Residue |
| A | SER114 |
| A | HIS292 |
| A | THR315 |
| A | HIS317 |
| A | LYS318 |
| A | ARG454 |
| A | HOH824 |
| B | TYR134 |
| B | GLU136 |
| B | TYR144 |
| B | GLY354 |
| A | SER180 |
| B | GLY355 |
| B | HOH706 |
| B | HOH787 |
| A | GLY181 |
| A | SER182 |
| A | HIS209 |
| A | ALA263 |
| A | SER264 |
| A | ASP289 |
| A | ALA291 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue EDO A 602 |
| Chain | Residue |
| A | GLN158 |
| A | LEU162 |
| A | GLY173 |
| A | VAL174 |
| A | HOH720 |
| site_id | AC3 |
| Number of Residues | 20 |
| Details | binding site for residue PLG B 601 |
| Chain | Residue |
| A | TYR134 |
| A | TYR144 |
| A | GLY354 |
| A | GLY355 |
| A | HOH745 |
| B | SER114 |
| B | SER180 |
| B | GLY181 |
| B | SER182 |
| B | HIS209 |
| B | ALA263 |
| B | SER264 |
| B | ASP289 |
| B | ALA291 |
| B | HIS292 |
| B | THR315 |
| B | HIS317 |
| B | LYS318 |
| B | ARG454 |
| B | HOH776 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | binding site for residue EDO B 602 |
| Chain | Residue |
| B | GLN159 |
| B | LEU162 |
| B | GLY173 |
| B | VAL174 |
| B | HOH711 |
| B | HOH760 |
| B | HOH768 |
| site_id | AC5 |
| Number of Residues | 8 |
| Details | binding site for residue ACT C 601 |
| Chain | Residue |
| C | SER180 |
| C | GLY181 |
| C | SER182 |
| C | THR315 |
| D | TYR134 |
| D | GLY354 |
| D | GLY355 |
| D | HOH766 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | binding site for residue ACT C 602 |
| Chain | Residue |
| C | SER114 |
| C | SER264 |
| C | HIS292 |
| C | LYS318 |
| C | ARG454 |
| D | GLU136 |
| D | TYR144 |
| site_id | AC7 |
| Number of Residues | 7 |
| Details | binding site for residue EDO C 603 |
| Chain | Residue |
| C | GLN158 |
| C | GLN159 |
| C | LEU162 |
| C | GLY173 |
| C | VAL174 |
| C | HOH702 |
| C | HOH711 |
| site_id | AC8 |
| Number of Residues | 21 |
| Details | binding site for residue PLS D 601 |
| Chain | Residue |
| C | TYR134 |
| C | GLU136 |
| C | TYR144 |
| C | GLY354 |
| C | GLY355 |
| C | HOH710 |
| D | SER114 |
| D | SER180 |
| D | GLY181 |
| D | SER182 |
| D | HIS209 |
| D | SER264 |
| D | ASP289 |
| D | ALA291 |
| D | HIS292 |
| D | THR315 |
| D | HIS317 |
| D | LYS318 |
| D | ARG454 |
| D | HOH718 |
| D | HOH752 |
| site_id | AC9 |
| Number of Residues | 8 |
| Details | binding site for residue EDO D 602 |
| Chain | Residue |
| D | LEU162 |
| D | GLY173 |
| D | VAL174 |
| D | HOH704 |
| D | HOH710 |
| D | HOH717 |
| D | GLN158 |
| D | GLN159 |
| site_id | AD1 |
| Number of Residues | 6 |
| Details | binding site for residue GLY E 601 |
| Chain | Residue |
| E | SER114 |
| E | HIS292 |
| E | LLP318 |
| E | ARG454 |
| F | GLU136 |
| F | TYR144 |
| site_id | AD2 |
| Number of Residues | 3 |
| Details | binding site for residue EDO E 602 |
| Chain | Residue |
| E | GLN158 |
| E | GLY173 |
| E | VAL174 |
| site_id | AD3 |
| Number of Residues | 20 |
| Details | binding site for residue PLG F 601 |
| Chain | Residue |
| E | TYR134 |
| E | GLU136 |
| E | TYR144 |
| E | GLY354 |
| E | GLY355 |
| E | HOH770 |
| F | SER114 |
| F | SER180 |
| F | GLY181 |
| F | SER182 |
| F | HIS209 |
| F | ALA263 |
| F | SER264 |
| F | ASP289 |
| F | HIS292 |
| F | THR315 |
| F | HIS317 |
| F | LYS318 |
| F | ARG454 |
| F | HOH810 |
| site_id | AD4 |
| Number of Residues | 8 |
| Details | binding site for residue EDO F 602 |
| Chain | Residue |
| F | GLN158 |
| F | GLN159 |
| F | LEU162 |
| F | GLY173 |
| F | VAL174 |
| F | HOH705 |
| F | HOH708 |
| F | HOH784 |
| site_id | AD5 |
| Number of Residues | 7 |
| Details | binding site for residue EDO G 601 |
| Chain | Residue |
| G | GLN158 |
| G | GLN159 |
| G | LEU162 |
| G | GLY173 |
| G | VAL174 |
| G | HOH703 |
| G | HOH797 |
| site_id | AD6 |
| Number of Residues | 6 |
| Details | binding site for residue ACT H 601 |
| Chain | Residue |
| G | SER114 |
| G | SER264 |
| G | HIS292 |
| G | ARG454 |
| H | GLU136 |
| H | TYR144 |
| site_id | AD7 |
| Number of Residues | 6 |
| Details | binding site for residue GLY H 602 |
| Chain | Residue |
| G | GLU136 |
| G | TYR144 |
| H | SER114 |
| H | HIS292 |
| H | LLP318 |
| H | ARG454 |
| site_id | AD8 |
| Number of Residues | 7 |
| Details | binding site for residue EDO H 603 |
| Chain | Residue |
| H | GLN158 |
| H | GLN159 |
| H | LEU162 |
| H | GLY173 |
| H | VAL174 |
| H | HOH719 |
| H | HOH729 |
Functional Information from PROSITE/UniProt
| site_id | PS00096 |
| Number of Residues | 17 |
| Details | SHMT Serine hydroxymethyltransferase pyridoxal-phosphate attachment site. DIvTTTTHKSLrGPRGG |
| Chain | Residue | Details |
| A | ASP310-GLY326 | |
| E | ASP310-GLY326 |
