3G8M
Serine Hydroxymethyltransferase Y55F Mutant
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004372 | molecular_function | glycine hydroxymethyltransferase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0006545 | biological_process | glycine biosynthetic process |
| A | 0006546 | biological_process | glycine catabolic process |
| A | 0006564 | biological_process | L-serine 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 | 0008732 | molecular_function | L-allo-threonine aldolase activity |
| A | 0016020 | cellular_component | membrane |
| A | 0016740 | molecular_function | transferase activity |
| A | 0019264 | biological_process | glycine biosynthetic process from L-serine |
| A | 0030170 | molecular_function | pyridoxal phosphate binding |
| A | 0035999 | biological_process | tetrahydrofolate interconversion |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0046653 | biological_process | tetrahydrofolate metabolic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE PLP A 418 |
| Chain | Residue |
| A | PHE55 |
| A | ARG235 |
| A | GLY263 |
| A | GLU57 |
| A | SER97 |
| A | GLY98 |
| A | SER99 |
| A | HIS126 |
| A | THR226 |
| A | HIS228 |
| A | LYS229 |
Functional Information from PROSITE/UniProt
| site_id | PS00096 |
| Number of Residues | 17 |
| Details | SHMT Serine hydroxymethyltransferase pyridoxal-phosphate attachment site. HVvTTTTHKTLaGPRGG |
| Chain | Residue | Details |
| A | HIS221-GLY237 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"10656824","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"10858298","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"1DFO","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1EQB","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"10656824","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"1DFO","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 5 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00051","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"10656824","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"10858298","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"1DFO","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1EQB","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"19883126","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3G8M","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Site: {"description":"Transaldimination and stability"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | Site: {"description":"Plays an important role in substrate specificity","evidences":[{"source":"HAMAP-Rule","id":"MF_00051","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"1517215","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 3 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"18723842","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 6 |
| Details | Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"PubMed","id":"21151122","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"source":"HAMAP-Rule","id":"MF_00051","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"19883126","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3G8M","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"PubMed","id":"21151122","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1dfo |
| Chain | Residue | Details |
| A | THR226 | |
| A | LYS229 | |
| A | GLU57 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1dfo |
| Chain | Residue | Details |
| A | LYS229 | |
| A | ASP200 | |
| A | HIS123 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1dfo |
| Chain | Residue | Details |
| A | LYS229 | |
| A | HIS203 |
| site_id | CSA4 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1dfo |
| Chain | Residue | Details |
| A | GLU69 |
