6LGO
Crystal structure of cystathionine gamma synthase from Xanthomonas oryzae pv. oryzae in complex with homolanthionine
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003962 | molecular_function | cystathionine gamma-synthase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0016846 | molecular_function | carbon-sulfur lyase activity |
| A | 0019346 | biological_process | transsulfuration |
| A | 0030170 | molecular_function | pyridoxal phosphate binding |
| B | 0003962 | molecular_function | cystathionine gamma-synthase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0016846 | molecular_function | carbon-sulfur lyase activity |
| B | 0019346 | biological_process | transsulfuration |
| B | 0030170 | molecular_function | pyridoxal phosphate binding |
| C | 0003962 | molecular_function | cystathionine gamma-synthase activity |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0016846 | molecular_function | carbon-sulfur lyase activity |
| C | 0019346 | biological_process | transsulfuration |
| C | 0030170 | molecular_function | pyridoxal phosphate binding |
| D | 0003962 | molecular_function | cystathionine gamma-synthase activity |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0016846 | molecular_function | carbon-sulfur lyase activity |
| D | 0019346 | biological_process | transsulfuration |
| D | 0030170 | molecular_function | pyridoxal phosphate binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 20 |
| Details | binding site for residue EBO A 501 |
| Chain | Residue |
| A | THR83 |
| A | LYS206 |
| A | GLY216 |
| A | GLU333 |
| A | SER334 |
| A | THR349 |
| A | ARG369 |
| B | ASP53 |
| B | TYR54 |
| B | ARG56 |
| B | SER57 |
| A | GLY84 |
| B | ASN235 |
| A | MET85 |
| A | TYR109 |
| A | ARG114 |
| A | ASN156 |
| A | ASP181 |
| A | SER203 |
| A | THR205 |
| site_id | AC2 |
| Number of Residues | 19 |
| Details | binding site for residue EBO B 501 |
| Chain | Residue |
| A | ASP53 |
| A | TYR54 |
| A | ARG56 |
| A | SER57 |
| A | ASN235 |
| B | THR83 |
| B | GLY84 |
| B | MET85 |
| B | TYR109 |
| B | ARG114 |
| B | ASN156 |
| B | ASP181 |
| B | SER203 |
| B | THR205 |
| B | LYS206 |
| B | GLU333 |
| B | SER334 |
| B | THR349 |
| B | ARG369 |
| site_id | AC3 |
| Number of Residues | 20 |
| Details | binding site for residue EBO C 501 |
| Chain | Residue |
| C | THR83 |
| C | GLY84 |
| C | MET85 |
| C | TYR109 |
| C | ARG114 |
| C | ASN156 |
| C | ASP181 |
| C | SER203 |
| C | THR205 |
| C | LYS206 |
| C | VAL215 |
| C | GLU333 |
| C | SER334 |
| C | THR349 |
| C | ARG369 |
| D | ASP53 |
| D | TYR54 |
| D | ARG56 |
| D | SER57 |
| D | ASN235 |
| site_id | AC4 |
| Number of Residues | 20 |
| Details | binding site for residue EBO D 501 |
| Chain | Residue |
| C | ASP53 |
| C | TYR54 |
| C | ARG56 |
| C | SER57 |
| C | ASN235 |
| C | HOH619 |
| D | THR83 |
| D | GLY84 |
| D | MET85 |
| D | TYR109 |
| D | ARG114 |
| D | ASN156 |
| D | ASP181 |
| D | SER203 |
| D | THR205 |
| D | LYS206 |
| D | GLU333 |
| D | SER334 |
| D | THR349 |
| D | ARG369 |
Functional Information from PROSITE/UniProt
| site_id | PS00868 |
| Number of Residues | 15 |
| Details | CYS_MET_METAB_PP Cys/Met metabolism enzymes pyridoxal-phosphate attachment site. DLvlhSTTKYInGHS |
| Chain | Residue | Details |
| A | ASP198-SER212 |
