1OAS
O-ACETYLSERINE SULFHYDRYLASE FROM SALMONELLA TYPHIMURIUM
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004124 | molecular_function | cysteine synthase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006535 | biological_process | cysteine biosynthetic process from serine |
| A | 0016740 | molecular_function | transferase activity |
| A | 0016765 | molecular_function | transferase activity, transferring alkyl or aryl (other than methyl) groups |
| A | 0019344 | biological_process | cysteine biosynthetic process |
| A | 0080146 | molecular_function | L-cysteine desulfhydrase activity |
| B | 0004124 | molecular_function | cysteine synthase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006535 | biological_process | cysteine biosynthetic process from serine |
| B | 0016740 | molecular_function | transferase activity |
| B | 0016765 | molecular_function | transferase activity, transferring alkyl or aryl (other than methyl) groups |
| B | 0019344 | biological_process | cysteine biosynthetic process |
| B | 0080146 | molecular_function | L-cysteine desulfhydrase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE PLP A 323 |
| Chain | Residue |
| A | GLY228 |
| A | ILE229 |
| A | SER272 |
| A | PRO299 |
| A | SER300 |
| A | TYR305 |
| A | HOH329 |
| A | HOH334 |
| A | HOH350 |
| A | HOH365 |
| A | LYS41 |
| A | ASN71 |
| A | GLY174 |
| A | GLY176 |
| A | THR177 |
| A | GLY178 |
| A | THR180 |
| site_id | AC2 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE PLP B 323 |
| Chain | Residue |
| B | LYS41 |
| B | ASN71 |
| B | GLY174 |
| B | VAL175 |
| B | GLY176 |
| B | THR177 |
| B | GLY178 |
| B | GLY179 |
| B | THR180 |
| B | GLY228 |
| B | ILE229 |
| B | SER272 |
| B | PRO299 |
| B | SER300 |
| B | TYR305 |
| B | HOH335 |
| B | HOH338 |
| B | HOH339 |
| site_id | PLP |
| Number of Residues | 2 |
| Details | SCHIFF-BASE LINKAGE TO COFACTOR |
| Chain | Residue |
| A | LYS41 |
| B | LYS41 |
Functional Information from PROSITE/UniProt
| site_id | PS00901 |
| Number of Residues | 19 |
| Details | CYS_SYNTHASE Cysteine synthase/cystathionine beta-synthase P-phosphate attachment site. KvEsrn.PSfSVKcRiGanM |
| Chain | Residue | Details |
| A | LYS30-MET48 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:11023792 |
| Chain | Residue | Details |
| A | ASN7 | |
| B | ASN7 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | BINDING: in other chain => ECO:0000305|PubMed:11023792 |
| Chain | Residue | Details |
| A | ARG34 | |
| A | LEU268 | |
| B | ARG34 | |
| B | LEU268 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:10452898, ECO:0000269|PubMed:11023792, ECO:0000269|PubMed:9761678 |
| Chain | Residue | Details |
| A | ASN71 | |
| A | SER272 | |
| B | ASN71 | |
| B | SER272 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | GLY176 | |
| B | GLY176 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | MOD_RES: N6-(pyridoxal phosphate)lysine |
| Chain | Residue | Details |
| A | LYS41 | |
| B | LYS41 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | a catalytic site defined by CSA, PubMed 11170356, 12515544 |
| Chain | Residue | Details |
| A | SER272 | |
| A | LYS41 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | a catalytic site defined by CSA, PubMed 11170356, 12515544 |
| Chain | Residue | Details |
| B | SER272 | |
| B | LYS41 |
| site_id | MCSA1 |
| Number of Residues | 2 |
| Details | M-CSA 865 |
| Chain | Residue | Details |
| A | LYS41 | covalent catalysis, proton shuttle (general acid/base) |
| A | SER272 | electrostatic stabiliser |
| site_id | MCSA2 |
| Number of Residues | 2 |
| Details | M-CSA 865 |
| Chain | Residue | Details |
| B | LYS41 | covalent catalysis, proton shuttle (general acid/base) |
| B | SER272 | electrostatic stabiliser |
