4IY7
crystal structure of cystathionine gamma lyase (XometC) from Xanthomonas oryzae pv. oryzae in complex with E-site serine, A-site external aldimine structure with serine and A-site external aldimine structure with aminoacrylate intermediates
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 | 8 |
| Details | BINDING SITE FOR RESIDUE SER A 401 |
| Chain | Residue |
| A | TYR112 |
| A | ARG117 |
| A | GLU338 |
| B | TYR58 |
| B | ARG60 |
| B | THR61 |
| B | ASN240 |
| B | HOH818 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL A 402 |
| Chain | Residue |
| A | ILE168 |
| A | ALA169 |
| A | ARG304 |
| A | GLN305 |
| C | ALA294 |
| C | SER295 |
| C | HOH699 |
| A | ASP167 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL A 403 |
| Chain | Residue |
| A | GLU280 |
| A | THR281 |
| A | HIS282 |
| A | ILE285 |
| D | ARG176 |
| D | LEU197 |
| D | SER198 |
| D | GLY200 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 A 404 |
| Chain | Residue |
| A | ARG117 |
| A | ARG121 |
| A | HOH630 |
| A | HOH704 |
| A | HOH837 |
| B | PHE237 |
| B | VAL300 |
| site_id | AC5 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE 0JO A 405 |
| Chain | Residue |
| A | SER87 |
| A | GLY88 |
| A | MET89 |
| A | TYR112 |
| A | ASN160 |
| A | ASP185 |
| A | SER207 |
| A | THR209 |
| A | LYS210 |
| A | SER339 |
| A | LEU340 |
| A | THR354 |
| A | ARG374 |
| B | TYR58 |
| B | ARG60 |
| site_id | AC6 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE SER B 401 |
| Chain | Residue |
| A | GLU57 |
| A | TYR58 |
| A | ARG60 |
| A | THR61 |
| A | ASN240 |
| B | TYR112 |
| B | ARG117 |
| B | GLU338 |
| B | KOU403 |
| B | HOH777 |
| site_id | AC7 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE PYR B 402 |
| Chain | Residue |
| A | ARG121 |
| A | ARG125 |
| B | GLN234 |
| B | PHE237 |
| B | LYS303 |
| B | HOH698 |
| B | HOH704 |
| site_id | AC8 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE KOU B 403 |
| Chain | Residue |
| A | TYR58 |
| A | ARG60 |
| B | SER87 |
| B | GLY88 |
| B | MET89 |
| B | TYR112 |
| B | ASN160 |
| B | ASP185 |
| B | SER207 |
| B | THR209 |
| B | LYS210 |
| B | GLU338 |
| B | SER339 |
| B | LEU340 |
| B | THR354 |
| B | ARG374 |
| B | SER401 |
| site_id | AC9 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE SER C 401 |
| Chain | Residue |
| C | TYR112 |
| C | ARG117 |
| C | GLU338 |
| C | KOU402 |
| C | HOH681 |
| D | GLU57 |
| D | TYR58 |
| D | ARG60 |
| D | THR61 |
| D | ASN240 |
| site_id | BC1 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE KOU C 402 |
| Chain | Residue |
| C | GLU338 |
| C | SER339 |
| C | THR354 |
| C | ARG374 |
| C | SER401 |
| D | TYR58 |
| D | ARG60 |
| C | SER87 |
| C | GLY88 |
| C | MET89 |
| C | TYR112 |
| C | ASN160 |
| C | ASP185 |
| C | SER207 |
| C | THR209 |
| C | LYS210 |
| site_id | BC2 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE SER D 401 |
| Chain | Residue |
| C | GLU57 |
| C | TYR58 |
| C | ARG60 |
| C | THR61 |
| C | ASN240 |
| D | TYR112 |
| D | ARG117 |
| D | GLU338 |
| D | KOU403 |
| site_id | BC3 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE PYR D 402 |
| Chain | Residue |
| D | ASN271 |
| D | ILE379 |
| D | GLU380 |
| D | ASP381 |
| D | LEU382 |
| D | HOH503 |
| D | HOH565 |
| D | HOH610 |
| D | HOH845 |
| site_id | BC4 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE KOU D 403 |
| Chain | Residue |
| C | TYR58 |
| C | ARG60 |
| D | SER87 |
| D | GLY88 |
| D | MET89 |
| D | TYR112 |
| D | ASN160 |
| D | ASP185 |
| D | SER207 |
| D | THR209 |
| D | LYS210 |
| D | SER339 |
| D | THR354 |
| D | ARG374 |
| D | SER401 |
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. DLvvhSATKYLnGHS |
| Chain | Residue | Details |
| A | ASP202-SER216 |
