6CZY
Crystal structure of Arabidopsis thaliana phosphoserine aminotransferase isoform 1 (AtPSAT1) in complex with Pyridoxamine-5'-phosphate (PMP)
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 | 18 |
| Details | binding site for residue PMP A 501 |
| Chain | Residue |
| A | GLY144 |
| A | GLN264 |
| A | LYS265 |
| A | HOH623 |
| A | HOH889 |
| B | ASN306 |
| B | THR307 |
| B | SO4503 |
| B | HOH716 |
| B | HOH745 |
| A | ALA145 |
| A | THR146 |
| A | TRP171 |
| A | CYS217 |
| A | ASN219 |
| A | THR221 |
| A | ASP241 |
| A | SER243 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue SO4 A 502 |
| Chain | Residue |
| A | GLY283 |
| A | ASN284 |
| A | LYS296 |
| A | HOH639 |
| A | HOH685 |
| A | HOH797 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | binding site for residue SO4 A 503 |
| Chain | Residue |
| A | HIS110 |
| A | ARG111 |
| A | HOH606 |
| A | HOH641 |
| A | HOH951 |
| B | TRP171 |
| B | PMP501 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | binding site for residue SO4 A 504 |
| Chain | Residue |
| A | SER170 |
| A | ASP173 |
| A | LYS192 |
| A | TYR196 |
| A | HOH619 |
| A | HOH734 |
| A | HOH895 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | binding site for residue PEG A 505 |
| Chain | Residue |
| A | GLY236 |
| A | PHE237 |
| A | ARG278 |
| A | HOH716 |
| A | HOH720 |
| A | HOH724 |
| site_id | AC6 |
| Number of Residues | 18 |
| Details | binding site for residue PMP B 501 |
| Chain | Residue |
| A | ASN306 |
| A | THR307 |
| A | SO4503 |
| A | HOH641 |
| A | HOH697 |
| B | GLY144 |
| B | ALA145 |
| B | THR146 |
| B | TRP171 |
| B | CYS217 |
| B | ASN219 |
| B | THR221 |
| B | ASP241 |
| B | SER243 |
| B | GLN264 |
| B | LYS265 |
| B | HOH608 |
| B | HOH903 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | binding site for residue SO4 B 502 |
| Chain | Residue |
| B | GLY283 |
| B | ASN284 |
| B | LYS296 |
| B | HOH614 |
| B | HOH670 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | binding site for residue SO4 B 503 |
| Chain | Residue |
| A | TRP171 |
| A | PMP501 |
| B | HIS110 |
| B | ARG111 |
| B | HOH716 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | binding site for residue NA B 504 |
| Chain | Residue |
| B | HOH610 |
| B | HOH992 |
| C | TRP189 |
| C | SER190 |
| C | HOH714 |
| C | HOH977 |
| site_id | AD1 |
| Number of Residues | 17 |
| Details | binding site for residue PMP C 501 |
| Chain | Residue |
| C | GLY144 |
| C | ALA145 |
| C | THR146 |
| C | TRP171 |
| C | CYS217 |
| C | ASN219 |
| C | THR221 |
| C | ASP241 |
| C | SER243 |
| C | GLN264 |
| C | LYS265 |
| C | HOH634 |
| C | HOH784 |
| C | HOH835 |
| D | ASN306 |
| D | THR307 |
| D | HOH661 |
| site_id | AD2 |
| Number of Residues | 7 |
| Details | binding site for residue MPD C 502 |
| Chain | Residue |
| D | HOH820 |
| D | HOH965 |
| D | HOH1044 |
| C | HIS110 |
| C | ARG111 |
| C | HOH739 |
| D | HIS396 |
| site_id | AD3 |
| Number of Residues | 7 |
| Details | binding site for residue SO4 C 503 |
| Chain | Residue |
| C | GLY283 |
| C | ASN284 |
| C | LYS296 |
| C | HOH610 |
| C | HOH620 |
| C | HOH636 |
| C | HOH657 |
| site_id | AD4 |
| Number of Residues | 7 |
| Details | binding site for residue PEG C 504 |
| Chain | Residue |
| C | GLY236 |
| C | PHE237 |
| C | ARG278 |
| C | HOH623 |
| C | HOH702 |
| C | HOH710 |
| C | HOH725 |
| site_id | AD5 |
| Number of Residues | 17 |
| Details | binding site for residue PMP D 501 |
| Chain | Residue |
| C | ASN306 |
| C | THR307 |
| D | GLY144 |
| D | ALA145 |
| D | THR146 |
| D | TRP171 |
| D | CYS217 |
| D | ASN219 |
| D | THR221 |
| D | ASP241 |
| D | SER243 |
| D | GLN264 |
| D | LYS265 |
| D | HOH753 |
| D | HOH754 |
| D | HOH820 |
| D | HOH867 |
| site_id | AD6 |
| Number of Residues | 6 |
| Details | binding site for residue SO4 D 502 |
| Chain | Residue |
| D | GLY283 |
| D | ASN284 |
| D | LYS296 |
| D | HOH671 |
| D | HOH816 |
| D | HOH930 |
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 |
