4WXB
Crystal Structure of Serine Hydroxymethyltransferase from Streptococcus thermophilus
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 | 0006545 | biological_process | glycine biosynthetic 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 |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0004372 | molecular_function | glycine hydroxymethyltransferase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006545 | biological_process | glycine biosynthetic 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 |
| C | 0003824 | molecular_function | catalytic activity |
| C | 0004372 | molecular_function | glycine hydroxymethyltransferase activity |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0006545 | biological_process | glycine biosynthetic process |
| C | 0006730 | biological_process | one-carbon metabolic process |
| C | 0008652 | biological_process | amino acid biosynthetic process |
| C | 0016740 | molecular_function | transferase activity |
| C | 0019264 | biological_process | glycine biosynthetic process from serine |
| C | 0030170 | molecular_function | pyridoxal phosphate binding |
| C | 0035999 | biological_process | tetrahydrofolate interconversion |
| D | 0003824 | molecular_function | catalytic activity |
| D | 0004372 | molecular_function | glycine hydroxymethyltransferase activity |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0006545 | biological_process | glycine biosynthetic process |
| D | 0006730 | biological_process | one-carbon metabolic process |
| D | 0008652 | biological_process | amino acid biosynthetic process |
| D | 0016740 | molecular_function | transferase 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 | 15 |
| Details | binding site for residue CIT A 501 |
| Chain | Residue |
| A | SER97 |
| A | HOH648 |
| A | HOH677 |
| C | TYR55 |
| C | HIS96 |
| C | GLN260 |
| C | GLY261 |
| A | GLY98 |
| A | SER99 |
| A | THR227 |
| A | HIS229 |
| A | LYS230 |
| A | ARG236 |
| A | CAC502 |
| A | HOH646 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | binding site for residue CAC A 502 |
| Chain | Residue |
| A | SER35 |
| A | LEU127 |
| A | HIS204 |
| A | LYS230 |
| A | ARG363 |
| A | CIT501 |
| C | TYR65 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | binding site for residue GOL A 503 |
| Chain | Residue |
| A | TYR59 |
| A | ILE79 |
| A | ALA91 |
| A | ASN92 |
| A | ASN252 |
| A | HOH633 |
| A | HOH700 |
| A | HOH712 |
| site_id | AC4 |
| Number of Residues | 11 |
| Details | binding site for residue CIT B 501 |
| Chain | Residue |
| B | SER97 |
| B | GLY98 |
| B | SER99 |
| B | THR227 |
| B | HIS229 |
| B | LYS230 |
| B | ARG236 |
| D | TYR55 |
| D | HIS96 |
| D | GLN260 |
| D | GLY261 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | binding site for residue CAC B 502 |
| Chain | Residue |
| B | SER35 |
| B | HIS204 |
| B | LYS230 |
| B | ARG363 |
| D | TYR65 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | binding site for residue NA B 503 |
| Chain | Residue |
| B | PHE301 |
| B | ASN302 |
| B | HIS304 |
| B | PHE307 |
| site_id | AC7 |
| Number of Residues | 9 |
| Details | binding site for residue GOL B 504 |
| Chain | Residue |
| B | TYR59 |
| B | LYS62 |
| B | ILE79 |
| B | ALA91 |
| B | ASN92 |
| B | ASN252 |
| B | HOH613 |
| B | HOH617 |
| B | HOH688 |
| site_id | AC8 |
| Number of Residues | 13 |
| Details | binding site for residue CIT C 501 |
| Chain | Residue |
| A | TYR55 |
| A | HIS96 |
| A | GLN260 |
| A | GLY261 |
| C | SER97 |
| C | GLY98 |
| C | SER99 |
| C | HIS229 |
| C | LYS230 |
| C | ARG236 |
| C | CAC502 |
| C | HOH671 |
| C | HOH716 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | binding site for residue CAC C 502 |
| Chain | Residue |
| A | TYR65 |
| C | SER35 |
| C | HIS204 |
| C | LYS230 |
| C | ARG363 |
| C | CIT501 |
| site_id | AD1 |
| Number of Residues | 4 |
| Details | binding site for residue NA C 503 |
| Chain | Residue |
| C | PHE301 |
| C | ASN302 |
| C | HIS304 |
| C | PHE307 |
| site_id | AD2 |
| Number of Residues | 6 |
| Details | binding site for residue GOL C 504 |
| Chain | Residue |
| C | TYR59 |
| C | ALA91 |
| C | ASN92 |
| C | ASN252 |
| C | HOH629 |
| C | HOH714 |
| site_id | AD3 |
| Number of Residues | 12 |
| Details | binding site for residue CIT D 501 |
| Chain | Residue |
| D | HOH634 |
| B | TYR55 |
| B | HIS96 |
| B | GLN260 |
| B | GLY261 |
| D | SER97 |
| D | GLY98 |
| D | SER99 |
| D | THR227 |
| D | HIS229 |
| D | LYS230 |
| D | ARG236 |
| site_id | AD4 |
| Number of Residues | 5 |
| Details | binding site for residue CAC D 502 |
| Chain | Residue |
| B | TYR55 |
| D | SER35 |
| D | HIS204 |
| D | LYS230 |
| D | ARG363 |
| site_id | AD5 |
| Number of Residues | 4 |
| Details | binding site for residue NA D 503 |
| Chain | Residue |
| D | PHE301 |
| D | ASN302 |
| D | HIS304 |
| D | PHE307 |
| site_id | AD6 |
| Number of Residues | 6 |
| Details | binding site for residue GOL D 504 |
| Chain | Residue |
| D | ILE79 |
| D | ALA91 |
| D | ASN92 |
| D | ASN252 |
| D | HOH608 |
| D | HOH651 |
Functional Information from PROSITE/UniProt
| site_id | PS00096 |
| Number of Residues | 17 |
| Details | SHMT Serine hydroxymethyltransferase pyridoxal-phosphate attachment site. HVtTTTTHKTLrGPRGG |
| Chain | Residue | Details |
| A | HIS222-GLY238 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00051 |
| Chain | Residue | Details |
| A | LEU121 | |
| D | LEU121 | |
| D | GLY125 | |
| D | SER355 | |
| A | GLY125 | |
| A | SER355 | |
| B | LEU121 | |
| B | GLY125 | |
| B | SER355 | |
| C | LEU121 | |
| C | GLY125 | |
| C | SER355 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | SITE: Plays an important role in substrate specificity => ECO:0000255|HAMAP-Rule:MF_00051 |
| Chain | Residue | Details |
| A | HIS229 | |
| B | HIS229 | |
| C | HIS229 | |
| D | HIS229 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | MOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000255|HAMAP-Rule:MF_00051 |
| Chain | Residue | Details |
| A | LYS230 | |
| B | LYS230 | |
| C | LYS230 | |
| D | LYS230 |
