6CD0
Crystal structure of Medicago truncatula serine hydroxymethyltransferase 3 (MtSHMT3), PLP-internal aldimine and apo form
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 |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | binding site for residue ACT A 601 |
Chain | Residue |
A | SER114 |
A | HIS292 |
A | LLP318 |
A | ARG454 |
B | TYR144 |
B | HOH707 |
site_id | AC2 |
Number of Residues | 9 |
Details | binding site for residue FMT B 601 |
Chain | Residue |
B | THR316 |
B | HIS317 |
B | LLP318 |
B | SER319 |
B | LEU320 |
B | HOH701 |
B | ALA291 |
B | SER294 |
B | THR315 |
site_id | AC3 |
Number of Residues | 7 |
Details | binding site for residue ACT B 602 |
Chain | Residue |
A | TYR144 |
A | HOH705 |
B | SER114 |
B | SER264 |
B | HIS292 |
B | LLP318 |
B | ARG454 |
site_id | AC4 |
Number of Residues | 8 |
Details | binding site for residue FMT C 601 |
Chain | Residue |
C | ALA291 |
C | SER294 |
C | THR315 |
C | THR316 |
C | HIS317 |
C | LYS318 |
C | SER319 |
C | LEU320 |
site_id | AC5 |
Number of Residues | 6 |
Details | binding site for residue ACT C 602 |
Chain | Residue |
C | SER180 |
C | GLY181 |
C | SER182 |
C | HOH1012 |
D | GLY354 |
D | FMT601 |
site_id | AC6 |
Number of Residues | 6 |
Details | binding site for residue FMT D 601 |
Chain | Residue |
C | SER180 |
C | ACT602 |
D | LEU179 |
D | GLN353 |
D | GLY354 |
D | GLY355 |
site_id | AC7 |
Number of Residues | 9 |
Details | binding site for residue FMT D 602 |
Chain | Residue |
D | ALA291 |
D | SER294 |
D | THR315 |
D | THR316 |
D | HIS317 |
D | LLP318 |
D | SER319 |
D | LEU320 |
D | HOH701 |
Functional Information from PROSITE/UniProt
site_id | PS00096 |
Number of Residues | 17 |
Details | SHMT Serine hydroxymethyltransferase pyridoxal-phosphate attachment site. DIvTTTTHKSLrGPRGG |
Chain | Residue | Details |
C | ASP310-GLY326 | |
A | ASP310-GLY326 |