6L0Q
Crystal Structure of the O-Phosphoserine Sulfhydrylase from Aeropyrum pernix Complexed with O-Phosphoserine
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 |
| C | 0004122 | molecular_function | cystathionine beta-synthase activity |
| C | 0004124 | molecular_function | cysteine synthase activity |
| C | 0008652 | biological_process | amino acid biosynthetic process |
| C | 0016740 | molecular_function | transferase activity |
| C | 0016829 | molecular_function | lyase activity |
| C | 0019344 | biological_process | cysteine biosynthetic process |
| C | 0033847 | molecular_function | O-phosphoserine sulfhydrylase activity |
| D | 0004122 | molecular_function | cystathionine beta-synthase activity |
| D | 0004124 | molecular_function | cysteine synthase activity |
| D | 0008652 | biological_process | amino acid biosynthetic process |
| D | 0016740 | molecular_function | transferase activity |
| D | 0016829 | molecular_function | lyase activity |
| D | 0019344 | biological_process | cysteine biosynthetic process |
| D | 0033847 | molecular_function | O-phosphoserine sulfhydrylase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 23 |
| Details | binding site for residue E1U A 401 |
| Chain | Residue |
| A | THR152 |
| A | THR262 |
| A | SER263 |
| A | GLY264 |
| A | HIS265 |
| A | GLY295 |
| A | ILE296 |
| A | ARG297 |
| A | SER341 |
| A | PRO368 |
| A | TYR374 |
| A | SER153 |
| A | HOH503 |
| A | HOH509 |
| A | HOH525 |
| A | HOH545 |
| A | ASN155 |
| A | PHE156 |
| A | THR203 |
| A | GLN224 |
| A | TYR225 |
| A | SER259 |
| A | GLY261 |
| site_id | AC2 |
| Number of Residues | 22 |
| Details | binding site for residue E1U B 401 |
| Chain | Residue |
| B | THR152 |
| B | SER153 |
| B | ASN155 |
| B | PHE156 |
| B | THR203 |
| B | GLN224 |
| B | TYR225 |
| B | SER259 |
| B | GLY261 |
| B | THR262 |
| B | SER263 |
| B | GLY264 |
| B | HIS265 |
| B | GLY295 |
| B | ILE296 |
| B | ARG297 |
| B | SER341 |
| B | PRO368 |
| B | HOH510 |
| B | HOH522 |
| B | HOH527 |
| B | HOH551 |
| site_id | AC3 |
| Number of Residues | 11 |
| Details | binding site for residue MPD B 402 |
| Chain | Residue |
| A | MET82 |
| A | PHE90 |
| A | GLY94 |
| A | PRO96 |
| A | THR97 |
| A | TYR119 |
| A | HOH508 |
| B | MET82 |
| B | GLY94 |
| B | TYR119 |
| B | HOH503 |
| site_id | AC4 |
| Number of Residues | 24 |
| Details | binding site for residue E1U C 401 |
| Chain | Residue |
| C | THR152 |
| C | SER153 |
| C | ASN155 |
| C | PHE156 |
| C | THR203 |
| C | GLN224 |
| C | TYR225 |
| C | SER259 |
| C | GLY261 |
| C | THR262 |
| C | SER263 |
| C | GLY264 |
| C | HIS265 |
| C | GLY295 |
| C | ILE296 |
| C | ARG297 |
| C | SER341 |
| C | PRO368 |
| C | ASP369 |
| C | TYR374 |
| C | HOH505 |
| C | HOH507 |
| C | HOH519 |
| C | HOH531 |
| site_id | AC5 |
| Number of Residues | 10 |
| Details | binding site for residue MPD C 402 |
| Chain | Residue |
| C | MET82 |
| C | PHE90 |
| C | GLY94 |
| C | PRO96 |
| C | THR97 |
| C | TYR119 |
| C | HOH502 |
| C | HOH516 |
| D | MET82 |
| D | TYR119 |
| site_id | AC6 |
| Number of Residues | 24 |
| Details | binding site for residue E1U D 401 |
| Chain | Residue |
| D | GLY261 |
| D | THR262 |
| D | SER263 |
| D | GLY264 |
| D | HIS265 |
| D | GLY295 |
| D | ILE296 |
| D | ARG297 |
| D | SER341 |
| D | PRO368 |
| D | TYR374 |
| D | HOH505 |
| D | HOH506 |
| D | HOH507 |
| D | HOH549 |
| D | THR152 |
| D | SER153 |
| D | ASN155 |
| D | PHE156 |
| D | THR203 |
| D | GLN224 |
| D | TYR225 |
| D | SER259 |
| D | LEU260 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"16005886","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 16 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"N6-(pyridoxal phosphate)lysine"} |
| Chain | Residue | Details |
