6CZX
Crystal structure of Arabidopsis thaliana phosphoserine aminotransferase isoform 1 (AtPSAT1) in complex with PLP internal aldimine
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004648 | molecular_function | O-phospho-L-serine:2-oxoglutarate aminotransferase activity |
| A | 0006564 | biological_process | L-serine biosynthetic process |
| B | 0004648 | molecular_function | O-phospho-L-serine:2-oxoglutarate aminotransferase activity |
| B | 0006564 | biological_process | L-serine biosynthetic process |
| C | 0004648 | molecular_function | O-phospho-L-serine:2-oxoglutarate aminotransferase activity |
| C | 0006564 | biological_process | L-serine biosynthetic process |
| D | 0004648 | molecular_function | O-phospho-L-serine:2-oxoglutarate aminotransferase activity |
| D | 0006564 | biological_process | L-serine biosynthetic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | binding site for residue SO4 A 501 |
| Chain | Residue |
| A | GLY283 |
| A | ASN284 |
| A | LYS296 |
| A | HOH612 |
| A | HOH733 |
| A | HOH869 |
| site_id | AC2 |
| Number of Residues | 10 |
| Details | binding site for residue SO4 A 502 |
| Chain | Residue |
| A | HOH616 |
| A | HOH625 |
| A | HOH640 |
| A | HOH658 |
| A | HOH697 |
| A | HOH716 |
| A | HOH819 |
| A | LYS180 |
| A | LYS184 |
| A | THR185 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | binding site for residue SO4 A 503 |
| Chain | Residue |
| A | SER170 |
| A | ASP173 |
| A | LYS192 |
| A | TYR196 |
| A | HOH677 |
| A | HOH767 |
| A | HOH850 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | binding site for residue SO4 A 504 |
| Chain | Residue |
| A | ASN86 |
| A | LEU318 |
| A | GLU321 |
| A | HOH604 |
| A | HOH732 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | binding site for residue SO4 A 505 |
| Chain | Residue |
| A | LYS174 |
| A | HIS396 |
| A | ARG397 |
| A | HOH605 |
| A | HOH877 |
| A | HOH907 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | binding site for residue PEG A 506 |
| Chain | Residue |
| A | GLY236 |
| A | ARG278 |
| A | HOH681 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | binding site for residue SO4 B 501 |
| Chain | Residue |
| B | GLY283 |
| B | ASN284 |
| B | LYS296 |
| B | HOH649 |
| B | HOH652 |
| B | HOH738 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 B 502 |
| Chain | Residue |
| A | GLN392 |
| B | GLY112 |
| B | LYS113 |
| B | HOH645 |
| site_id | AC9 |
| Number of Residues | 9 |
| Details | binding site for residue PEG B 503 |
| Chain | Residue |
| B | LYS228 |
| B | GLN337 |
| B | ASP341 |
| B | LYS360 |
| B | SER361 |
| B | ARG363 |
| B | LEU365 |
| B | HOH914 |
| B | HOH975 |
| site_id | AD1 |
| Number of Residues | 6 |
| Details | binding site for residue MRD B 504 |
| Chain | Residue |
| A | HOH793 |
| A | HOH877 |
| A | HOH999 |
| B | HIS110 |
| B | ARG111 |
| B | HOH741 |
| site_id | AD2 |
| Number of Residues | 6 |
| Details | binding site for residue SO4 C 501 |
| Chain | Residue |
| C | GLY283 |
| C | ASN284 |
| C | LYS296 |
| C | HOH630 |
| C | HOH634 |
| C | HOH673 |
| site_id | AD3 |
| Number of Residues | 10 |
| Details | binding site for residue SO4 C 502 |
| Chain | Residue |
| C | LYS180 |
| C | LYS184 |
| C | THR185 |
| C | HOH644 |
| C | HOH665 |
| C | HOH700 |
| C | HOH716 |
| C | HOH741 |
| C | HOH842 |
| C | HOH849 |
| site_id | AD4 |
| Number of Residues | 6 |
| Details | binding site for residue SO4 C 503 |
| Chain | Residue |
| C | SER170 |
| C | ASP173 |
| C | LYS192 |
| C | TYR196 |
| C | HOH768 |
| C | HOH774 |
| site_id | AD5 |
| Number of Residues | 5 |
| Details | binding site for residue SO4 C 504 |
| Chain | Residue |
| C | LYS174 |
| C | HIS396 |
| C | ARG397 |
| C | HOH607 |
| C | HOH766 |
| site_id | AD6 |
| Number of Residues | 7 |
| Details | binding site for residue PEG C 505 |
| Chain | Residue |
| C | GLY236 |
| C | PHE237 |
| C | ARG278 |
| C | HOH643 |
| C | HOH723 |
| C | HOH737 |
| C | HOH934 |
| site_id | AD7 |
| Number of Residues | 8 |
| Details | binding site for residue MRD C 506 |
| Chain | Residue |
| C | HOH1039 |
| D | HIS396 |
| D | HOH723 |
| D | HOH943 |
| D | HOH982 |
| C | HIS110 |
| C | ARG111 |
| C | HOH810 |
| site_id | AD8 |
| Number of Residues | 6 |
| Details | binding site for residue SO4 D 501 |
| Chain | Residue |
| D | GLY283 |
| D | ASN284 |
| D | LYS296 |
| D | HOH636 |
| D | HOH660 |
| D | HOH700 |
Functional Information from PROSITE/UniProt
| site_id | PS00595 |
| Number of Residues | 20 |
| Details | AA_TRANSFER_CLASS_5 Aminotransferases class-V pyridoxal-phosphate attachment site. FGVIygGAQKnvgps.GvTiV |
| Chain | Residue | Details |
| A | PHE256-VAL275 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 20 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"30034403","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6CZY","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6CZZ","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"30034403","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6CZZ","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"source":"PubMed","id":"30034403","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6CZY","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6CZZ","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
