3VSC
Crystal Structure of the K127A Mutant of O-Phosphoserine Sulfhydrylase Complexed with External Schiff Base of Pyridoxal 5'-Phosphate with O-Phospho-L-Serine
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004122 | molecular_function | cystathionine beta-synthase activity |
| A | 0004124 | molecular_function | cysteine synthase activity |
| A | 0008652 | biological_process | amino acid biosynthetic process |
| A | 0016740 | molecular_function | transferase activity |
| A | 0016829 | molecular_function | lyase activity |
| A | 0019344 | biological_process | cysteine biosynthetic process |
| A | 0033847 | molecular_function | O-phosphoserine sulfhydrylase activity |
| B | 0004122 | molecular_function | cystathionine beta-synthase activity |
| B | 0004124 | molecular_function | cysteine synthase activity |
| B | 0008652 | biological_process | amino acid biosynthetic process |
| B | 0016740 | molecular_function | transferase activity |
| B | 0016829 | molecular_function | lyase activity |
| B | 0019344 | biological_process | cysteine biosynthetic process |
| B | 0033847 | molecular_function | O-phosphoserine sulfhydrylase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE PLP A 401 |
| Chain | Residue |
| A | ASN155 |
| A | ILE296 |
| A | SER341 |
| A | PRO368 |
| A | ASP369 |
| A | TYR374 |
| A | SEP402 |
| A | HOH502 |
| A | HOH516 |
| A | HOH532 |
| A | HOH569 |
| A | SER259 |
| A | LEU260 |
| A | GLY261 |
| A | THR262 |
| A | SER263 |
| A | GLY264 |
| A | HIS265 |
| A | GLY295 |
| site_id | AC2 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE SEP A 402 |
| Chain | Residue |
| A | THR152 |
| A | SER153 |
| A | ASN155 |
| A | PHE156 |
| A | THR203 |
| A | GLN224 |
| A | PHE225 |
| A | GLY261 |
| A | THR262 |
| A | GLY295 |
| A | PLP401 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE MPD A 403 |
| Chain | Residue |
| A | MET82 |
| A | GLY94 |
| A | PRO96 |
| A | THR97 |
| B | MET82 |
| B | TYR119 |
| B | HOH524 |
| site_id | AC4 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE PLP B 401 |
| Chain | Residue |
| B | ASN155 |
| B | SER259 |
| B | GLY261 |
| B | THR262 |
| B | SER263 |
| B | GLY264 |
| B | HIS265 |
| B | GLY295 |
| B | ILE296 |
| B | SER341 |
| B | PRO368 |
| B | TYR374 |
| B | SEP402 |
| B | HOH501 |
| B | HOH541 |
| B | HOH567 |
| site_id | AC5 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE SEP B 402 |
| Chain | Residue |
| B | THR152 |
| B | SER153 |
| B | ASN155 |
| B | PHE156 |
| B | THR203 |
| B | GLN224 |
| B | PHE225 |
| B | GLY261 |
| B | THR262 |
| B | GLY295 |
| B | ARG297 |
| B | PLP401 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"16005886","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-(pyridoxal phosphate)lysine"} |
| Chain | Residue | Details |
