2VIB
Crystal structure of S172AbsSHMT obtained in the presence of L-allo- Thr
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 | 0005829 | cellular_component | cytosol |
| A | 0006545 | biological_process | glycine biosynthetic process |
| A | 0006565 | biological_process | L-serine catabolic process |
| A | 0006730 | biological_process | one-carbon metabolic process |
| A | 0008270 | molecular_function | zinc ion binding |
| 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 |
| A | 0046655 | biological_process | folic acid metabolic process |
| A | 0050897 | molecular_function | cobalt ion binding |
| A | 0070905 | molecular_function | serine binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE PLP A1406 |
| Chain | Residue |
| A | TYR51 |
| A | HIS200 |
| A | THR223 |
| A | HIS225 |
| A | LYS226 |
| A | GLY256 |
| A | GLY257 |
| A | GLY1407 |
| A | HOH2080 |
| A | HOH2410 |
| A | HOH2411 |
| A | SER93 |
| A | GLY94 |
| A | ALA95 |
| A | HIS122 |
| A | ALA171 |
| A | ALA172 |
| A | ASP197 |
| A | ALA199 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GLY A1407 |
| Chain | Residue |
| A | SER31 |
| A | TYR51 |
| A | TYR61 |
| A | HIS122 |
| A | HIS200 |
| A | LYS226 |
| A | ARG357 |
| A | PLP1406 |
| site_id | AC3 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE MPD A1408 |
| Chain | Residue |
| A | TYR152 |
| A | ARG156 |
| A | GLN321 |
| A | LEU322 |
| A | VAL387 |
| A | HOH2229 |
| A | HOH2326 |
| A | HOH2412 |
| A | HOH2413 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MPD A1409 |
| Chain | Residue |
| A | PHE131 |
| A | GLN135 |
| A | TYR136 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PO4 A1410 |
| Chain | Residue |
| A | GLU371 |
| A | GLU375 |
| A | HOH2372 |
| A | HOH2414 |
Functional Information from PROSITE/UniProt
| site_id | PS00096 |
| Number of Residues | 17 |
| Details | SHMT Serine hydroxymethyltransferase pyridoxal-phosphate attachment site. HFvTTTTHKTLrGPRGG |
| Chain | Residue | Details |
| A | HIS218-GLY234 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1dfo |
| Chain | Residue | Details |
| A | LYS226 | |
| A | THR223 | |
| A | GLU53 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1dfo |
| Chain | Residue | Details |
| A | LYS226 | |
| A | HIS119 | |
| A | ASP197 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1dfo |
| Chain | Residue | Details |
| A | LYS226 | |
| A | HIS200 |
| site_id | CSA4 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1dfo |
| Chain | Residue | Details |
| A | GLU65 |
