2VMY
Crystal structure of F351GbsSHMT in complex with Gly and FTHF
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004372 | molecular_function | glycine hydroxymethyltransferase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0006544 | biological_process | glycine metabolic process |
| A | 0006545 | biological_process | glycine biosynthetic process |
| A | 0006563 | biological_process | L-serine metabolic 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 |
| A | 0046653 | biological_process | tetrahydrofolate metabolic process |
| B | 0004372 | molecular_function | glycine hydroxymethyltransferase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0006544 | biological_process | glycine metabolic process |
| B | 0006545 | biological_process | glycine biosynthetic process |
| B | 0006563 | biological_process | L-serine metabolic 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 |
| B | 0046653 | biological_process | tetrahydrofolate metabolic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE PLP A 501 |
| Chain | Residue |
| A | SER93 |
| A | THR223 |
| A | HIS225 |
| A | LYS226 |
| A | GLY502 |
| B | TYR51 |
| B | GLY256 |
| B | GLY257 |
| A | GLY94 |
| A | ALA95 |
| A | HIS122 |
| A | ALA171 |
| A | SER172 |
| A | ASP197 |
| A | ALA199 |
| A | HIS200 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GLY A 502 |
| Chain | Residue |
| A | SER31 |
| A | HIS200 |
| A | LYS226 |
| A | ARG357 |
| A | PLP501 |
| B | TYR51 |
| B | TYR61 |
| B | FFO505 |
| site_id | AC3 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE FFO A 505 |
| Chain | Residue |
| A | GLU53 |
| A | TYR60 |
| A | TYR61 |
| A | LYS248 |
| A | PHE251 |
| B | LEU117 |
| B | GLY120 |
| B | GLY121 |
| B | HIS122 |
| B | LEU123 |
| B | VAL129 |
| B | SER172 |
| B | ASN341 |
| B | SER349 |
| B | PRO350 |
| B | GLY351 |
| B | GLY502 |
| site_id | AC4 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE PLP B 501 |
| Chain | Residue |
| A | TYR51 |
| A | GLY256 |
| A | GLY257 |
| B | SER93 |
| B | GLY94 |
| B | ALA95 |
| B | HIS122 |
| B | ALA171 |
| B | SER172 |
| B | ASP197 |
| B | ALA199 |
| B | HIS200 |
| B | THR223 |
| B | HIS225 |
| B | LYS226 |
| B | GLY502 |
| B | HOH2003 |
| site_id | AC5 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GLY B 502 |
| Chain | Residue |
| A | TYR51 |
| A | TYR61 |
| A | FFO505 |
| B | SER31 |
| B | HIS200 |
| B | LYS226 |
| B | ARG357 |
| B | PLP501 |
| site_id | AC6 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE FFO B 505 |
| Chain | Residue |
| A | LEU117 |
| A | GLY120 |
| A | GLY121 |
| A | HIS122 |
| A | LEU123 |
| A | VAL129 |
| A | ASN339 |
| A | ASN341 |
| A | SER349 |
| A | PRO350 |
| A | GLY351 |
| A | ARG357 |
| A | GLY502 |
| B | GLU53 |
| B | TYR60 |
| B | TYR61 |
| B | PHE251 |
| site_id | AC7 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE MRD B 701 |
| Chain | Residue |
| A | TYR136 |
| B | GLN135 |
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 |
| B | LYS226 | |
| B | THR223 | |
| B | GLU53 |
| site_id | CSA3 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1dfo |
| Chain | Residue | Details |
| A | LYS226 | |
| A | HIS119 | |
| A | ASP197 |
| site_id | CSA4 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1dfo |
| Chain | Residue | Details |
| B | LYS226 | |
| B | HIS119 | |
| B | ASP197 |
| site_id | CSA5 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1dfo |
| Chain | Residue | Details |
| A | LYS226 | |
| A | HIS200 |
| site_id | CSA6 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1dfo |
| Chain | Residue | Details |
| B | LYS226 | |
| B | HIS200 |
| site_id | CSA7 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1dfo |
| Chain | Residue | Details |
| A | GLU65 |
| site_id | CSA8 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1dfo |
| Chain | Residue | Details |
| B | GLU65 |
