1WKV
Crystal structure of O-phosphoserine sulfhydrylase
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 | 0006535 | biological_process | cysteine biosynthetic process from serine |
| 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 | 0006535 | biological_process | cysteine biosynthetic process from serine |
| 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 | 7 |
| Details | BINDING SITE FOR RESIDUE ACT A 1401 |
| Chain | Residue |
| A | THR152 |
| A | SER153 |
| A | THR203 |
| A | GLN224 |
| A | PHE225 |
| A | HOH1417 |
| A | HOH1470 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ACT B 2401 |
| Chain | Residue |
| B | SER153 |
| B | GLN224 |
| B | HOH2413 |
| B | HOH2519 |
| B | LYS127 |
| B | THR152 |
| site_id | AC3 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE PLP A 400 |
| Chain | Residue |
| A | LYS127 |
| A | ASN155 |
| A | SER259 |
| A | GLY261 |
| A | THR262 |
| A | SER263 |
| A | GLY264 |
| A | HIS265 |
| A | GLY295 |
| A | ILE296 |
| A | SER341 |
| A | PRO368 |
| A | ASP369 |
| A | HOH1402 |
| A | HOH1412 |
| A | HOH1415 |
| site_id | AC4 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE PLP B 400 |
| Chain | Residue |
| B | LYS127 |
| B | ASN155 |
| B | SER259 |
| B | LEU260 |
| B | GLY261 |
| B | THR262 |
| B | SER263 |
| B | GLY264 |
| B | HIS265 |
| B | ILE296 |
| B | SER341 |
| B | PRO368 |
| B | ASP369 |
| B | HOH2402 |
| B | HOH2407 |
| B | HOH2409 |
Functional Information from PROSITE/UniProt
| site_id | PS00901 |
| Number of Residues | 20 |
| Details | CYS_SYNTHASE Cysteine synthase/cystathionine beta-synthase P-phosphate attachment site. KlEwynpFSlSVKdRpAveI |
| Chain | Residue | Details |
| A | LYS115-ILE134 |
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 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1oas |
| Chain | Residue | Details |
| A | LYS127 | |
| A | SER341 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1oas |
| Chain | Residue | Details |
| B | LYS127 | |
| B | SER341 |
| site_id | CSA3 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1oas |
| Chain | Residue | Details |
| A | LYS127 |
| site_id | CSA4 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1oas |
| Chain | Residue | Details |
| B | LYS127 |
