2JG2
HIGH RESOLUTION STRUCTURE OF SPT WITH PLP INTERNAL ALDIMINE
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004758 | molecular_function | serine C-palmitoyltransferase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006629 | biological_process | lipid metabolic process |
| A | 0006665 | biological_process | sphingolipid metabolic process |
| A | 0009058 | biological_process | biosynthetic process |
| A | 0016020 | cellular_component | membrane |
| A | 0016740 | molecular_function | transferase activity |
| A | 0016746 | molecular_function | acyltransferase activity |
| A | 0030170 | molecular_function | pyridoxal phosphate binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE PLP A 1265 |
| Chain | Residue |
| A | GLY134 |
| A | SER264 |
| A | LYS265 |
| A | GLY271 |
| A | THR294 |
| A | ALA295 |
| A | HOH2290 |
| A | TYR135 |
| A | ASN138 |
| A | HIS159 |
| A | SER161 |
| A | GLU202 |
| A | ASP231 |
| A | HIS234 |
| A | THR262 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG A 1421 |
| Chain | Residue |
| A | HOH2030 |
| A | HOH2062 |
| A | HOH2064 |
| A | HOH2102 |
| A | HOH2104 |
Functional Information from PROSITE/UniProt
| site_id | PS00599 |
| Number of Residues | 10 |
| Details | AA_TRANSFER_CLASS_2 Aminotransferases class-II pyridoxal-phosphate attachment site. TFSKSVGTVG |
| Chain | Residue | Details |
| A | THR262-GLY271 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"17559874","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19376777","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2JG2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2W8T","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2W8U","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2W8V","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"17559874","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2JG2","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"source":"PubMed","id":"17559874","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19376777","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2JG2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2W8T","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2W8U","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2W8V","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1bs0 |
| Chain | Residue | Details |
| A | ASP231 | |
| A | HIS159 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1bs0 |
| Chain | Residue | Details |
| A | ASN106 |
| site_id | CSA3 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1bs0 |
| Chain | Residue | Details |
| A | ASP231 | |
| A | HIS159 | |
| A | GLU202 |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1bs0 |
| Chain | Residue | Details |
| A | TYR135 | |
| A | ASP231 |
| site_id | CSA5 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1bs0 |
| Chain | Residue | Details |
| A | HIS234 |
| site_id | CSA6 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1bs0 |
| Chain | Residue | Details |
| A | ARG103 |
