6L0S
Crystal Structure of the O-Phosphoserine Sulfhydrylase from Aeropyrum pernix Complexed with L-Cysteine
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 | 17 |
| Details | binding site for residue E1O A 401 |
| Chain | Residue |
| A | THR152 |
| A | GLY264 |
| A | HIS265 |
| A | GLY295 |
| A | ILE296 |
| A | SER341 |
| A | PRO368 |
| A | ASP369 |
| A | HOH502 |
| A | SER153 |
| A | ASN155 |
| A | PHE156 |
| A | GLN224 |
| A | SER259 |
| A | GLY261 |
| A | THR262 |
| A | SER263 |
| site_id | AC2 |
| Number of Residues | 9 |
| Details | binding site for residue MPD A 402 |
| Chain | Residue |
| A | MET82 |
| A | PHE90 |
| A | GLY94 |
| A | PRO96 |
| A | THR97 |
| A | TYR119 |
| A | HOH503 |
| B | MET82 |
| B | TYR119 |
| site_id | AC3 |
| Number of Residues | 19 |
| Details | binding site for residue E1O B 401 |
| Chain | Residue |
| B | THR152 |
| B | SER153 |
| B | ASN155 |
| B | PHE156 |
| B | GLN224 |
| B | TYR225 |
| B | SER259 |
| B | LEU260 |
| B | GLY261 |
| B | THR262 |
| B | SER263 |
| B | GLY264 |
| B | HIS265 |
| B | GLY295 |
| B | ILE296 |
| B | SER341 |
| B | PRO368 |
| B | TYR374 |
| B | HOH501 |
| site_id | AC4 |
| Number of Residues | 20 |
| Details | binding site for residue E1O C 401 |
| Chain | Residue |
| C | THR152 |
| C | SER153 |
| C | ASN155 |
| C | PHE156 |
| C | GLN224 |
| C | TYR225 |
| C | SER259 |
| C | LEU260 |
| C | GLY261 |
| C | THR262 |
| C | SER263 |
| C | GLY264 |
| C | HIS265 |
| C | GLY295 |
| C | ILE296 |
| C | SER341 |
| C | PRO368 |
| C | ASP369 |
| C | TYR374 |
| C | HOH507 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | binding site for residue MPD C 402 |
| Chain | Residue |
| C | MET82 |
| C | GLY94 |
| C | PRO96 |
| C | THR97 |
| C | HOH503 |
| D | MET82 |
| D | TYR119 |
| site_id | AC6 |
| Number of Residues | 19 |
| Details | binding site for residue E1O D 401 |
| Chain | Residue |
| D | THR152 |
| D | SER153 |
| D | ASN155 |
| D | PHE156 |
| D | GLN224 |
| D | TYR225 |
| D | SER259 |
| D | LEU260 |
| D | GLY261 |
| D | THR262 |
| D | SER263 |
| D | GLY264 |
| D | HIS265 |
| D | GLY295 |
| D | ILE296 |
| D | SER341 |
| D | PRO368 |
| D | ASP369 |
| D | HOH501 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:16005886 |
| Chain | Residue | Details |
| A | ASN155 | |
| A | SER341 | |
| B | ASN155 | |
| B | SER341 | |
| C | ASN155 | |
| C | SER341 | |
| D | ASN155 | |
| D | SER341 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | GLY261 | |
| B | GLY261 | |
| C | GLY261 | |
| D | GLY261 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | MOD_RES: N6-(pyridoxal phosphate)lysine |
| Chain | Residue | Details |
| A | ALA127 | |
| B | ALA127 | |
| C | ALA127 | |
| D | ALA127 |
