1KL2
Crystal Structure of Serine Hydroxymethyltransferase Complexed with Glycine and 5-formyl tetrahydrofolate
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 | 14 |
Details | BINDING SITE FOR RESIDUE PLP A 501 |
Chain | Residue |
A | SER93 |
A | HIS225 |
A | LYS226 |
A | GLY601 |
B | TYR51 |
B | GLY257 |
A | GLY94 |
A | ALA95 |
A | HIS122 |
A | SER172 |
A | ASP197 |
A | ALA199 |
A | HIS200 |
A | THR223 |
site_id | AC2 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE GLY A 601 |
Chain | Residue |
A | SER31 |
A | HIS122 |
A | SER172 |
A | HIS200 |
A | LYS226 |
A | ARG357 |
A | PLP501 |
A | FON505 |
B | TYR51 |
B | TYR61 |
site_id | AC3 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE PLP B 502 |
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 | GLY602 |
B | HOH633 |
site_id | AC4 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GLY B 602 |
Chain | Residue |
A | TYR51 |
A | TYR61 |
B | SER31 |
B | HIS200 |
B | LYS226 |
B | ARG357 |
B | PLP502 |
site_id | AC5 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE FON A 505 |
Chain | Residue |
A | LEU117 |
A | GLY121 |
A | HIS122 |
A | LEU123 |
A | SER172 |
A | ASN341 |
A | GLY601 |
B | GLU53 |
B | ARG58 |
B | TYR60 |
B | TYR61 |
B | PHE251 |
site_id | AC6 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE FON B 506 |
Chain | Residue |
A | GLU53 |
A | TYR60 |
A | TYR61 |
A | PHE251 |
B | LEU117 |
B | GLY120 |
B | GLY121 |
B | HIS122 |
B | LEU123 |
B | SER172 |
B | ASN341 |
B | SER349 |
B | PHE351 |
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 | 1 |
Details | Annotated By Reference To The Literature 1dfo |
Chain | Residue | Details |
A | CYS64 |
site_id | CSA10 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1dfo |
Chain | Residue | Details |
B | GLU65 |
site_id | CSA2 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1dfo |
Chain | Residue | Details |
B | CYS64 |
site_id | CSA3 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1dfo |
Chain | Residue | Details |
A | LYS226 | |
A | THR223 | |
A | GLU53 |
site_id | CSA4 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1dfo |
Chain | Residue | Details |
B | LYS226 | |
B | THR223 | |
B | GLU53 |
site_id | CSA5 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1dfo |
Chain | Residue | Details |
A | LYS226 | |
A | HIS119 | |
A | ASP197 |
site_id | CSA6 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1dfo |
Chain | Residue | Details |
B | LYS226 | |
B | HIS119 | |
B | ASP197 |
site_id | CSA7 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1dfo |
Chain | Residue | Details |
A | LYS226 | |
A | HIS200 |
site_id | CSA8 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1dfo |
Chain | Residue | Details |
B | LYS226 | |
B | HIS200 |
site_id | CSA9 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1dfo |
Chain | Residue | Details |
A | GLU65 |