4IYO
Crystal structure of cystathionine gamma lyase from Xanthomonas oryzae pv. oryzae (XometC) in complex with E-site serine, A-site serine, A-site external aldimine structure with aminoacrylate and A-site iminopropionate intermediates
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000096 | biological_process | sulfur amino acid metabolic process |
| A | 0003962 | molecular_function | cystathionine gamma-synthase activity |
| A | 0004123 | molecular_function | cystathionine gamma-lyase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0016846 | molecular_function | carbon-sulfur lyase activity |
| A | 0019343 | biological_process | cysteine biosynthetic process via cystathionine |
| A | 0019346 | biological_process | transsulfuration |
| A | 0030170 | molecular_function | pyridoxal phosphate binding |
| B | 0000096 | biological_process | sulfur amino acid metabolic process |
| B | 0003962 | molecular_function | cystathionine gamma-synthase activity |
| B | 0004123 | molecular_function | cystathionine gamma-lyase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0016846 | molecular_function | carbon-sulfur lyase activity |
| B | 0019343 | biological_process | cysteine biosynthetic process via cystathionine |
| B | 0019346 | biological_process | transsulfuration |
| B | 0030170 | molecular_function | pyridoxal phosphate binding |
| C | 0000096 | biological_process | sulfur amino acid metabolic process |
| C | 0003962 | molecular_function | cystathionine gamma-synthase activity |
| C | 0004123 | molecular_function | cystathionine gamma-lyase activity |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0016846 | molecular_function | carbon-sulfur lyase activity |
| C | 0019343 | biological_process | cysteine biosynthetic process via cystathionine |
| C | 0019346 | biological_process | transsulfuration |
| C | 0030170 | molecular_function | pyridoxal phosphate binding |
| D | 0000096 | biological_process | sulfur amino acid metabolic process |
| D | 0003962 | molecular_function | cystathionine gamma-synthase activity |
| D | 0004123 | molecular_function | cystathionine gamma-lyase activity |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0016846 | molecular_function | carbon-sulfur lyase activity |
| D | 0019343 | biological_process | cysteine biosynthetic process via cystathionine |
| D | 0019346 | biological_process | transsulfuration |
| D | 0030170 | molecular_function | pyridoxal phosphate binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SER A 401 |
| Chain | Residue |
| A | TYR112 |
| A | ARG117 |
| A | GLU338 |
| B | TYR58 |
| B | ARG60 |
| B | THR61 |
| B | ASN240 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL A 402 |
| Chain | Residue |
| A | ALA169 |
| A | ARG304 |
| A | GLN305 |
| C | ALA294 |
| C | SER295 |
| C | HOH675 |
| A | ASP167 |
| A | ILE168 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 A 403 |
| Chain | Residue |
| A | ARG117 |
| A | HOH640 |
| A | HOH694 |
| B | PHE237 |
| B | VAL300 |
| B | ARG304 |
| site_id | AC4 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE 0JO A 404 |
| Chain | Residue |
| A | SER87 |
| A | GLY88 |
| A | MET89 |
| A | TYR112 |
| A | ASN160 |
| A | ASP185 |
| A | PHE188 |
| A | SER207 |
| A | THR209 |
| A | LYS210 |
| A | SER339 |
| A | LEU340 |
| A | THR354 |
| A | ARG374 |
| B | TYR58 |
| B | ARG60 |
| site_id | AC5 |
| Number of Residues | 9 |
| 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 | NAK402 |
| site_id | AC6 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE NAK B 402 |
| Chain | Residue |
| A | TYR58 |
| B | TYR112 |
| B | ASN160 |
| B | LLP210 |
| B | SER339 |
| B | LEU340 |
| B | THR354 |
| B | ARG374 |
| B | SER401 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PYR B 403 |
| Chain | Residue |
| B | GLN234 |
| B | PHE237 |
| B | LYS303 |
| B | ARG304 |
| B | HOH673 |
| B | HOH710 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SER C 401 |
| Chain | Residue |
| C | TYR112 |
| C | ARG117 |
| C | GLU338 |
| D | TYR58 |
| D | ARG60 |
| D | THR61 |
| D | ASN240 |
| site_id | AC9 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE NAK C 402 |
| Chain | Residue |
| C | TYR112 |
| C | ASN160 |
| C | LLP210 |
| C | SER339 |
| C | THR354 |
| C | ARG374 |
| D | TYR58 |
| site_id | BC1 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE GOL C 403 |
| Chain | Residue |
| A | ALA18 |
| A | HOH813 |
| C | ALA267 |
| C | ASN271 |
| C | ILE379 |
| C | GLU380 |
| C | HOH568 |
| C | HOH580 |
| C | HOH597 |
| C | HOH603 |
| C | HOH726 |
| site_id | BC2 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE SER D 401 |
| Chain | Residue |
| C | TYR58 |
| C | ARG60 |
| C | THR61 |
| C | ASN240 |
| C | HOH745 |
| D | TYR112 |
| D | ARG117 |
| D | GLU338 |
| D | SER402 |
| D | HOH835 |
| site_id | BC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SER D 402 |
| Chain | Residue |
| D | SER339 |
| D | THR354 |
| D | ARG374 |
| D | SER401 |
| D | TYR112 |
| D | ASN160 |
| D | LLP210 |
| site_id | BC4 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL D 403 |
| Chain | Residue |
| D | PHE67 |
| D | GLU70 |
| D | ARG71 |
| D | HOH522 |
| D | HOH542 |
| D | HOH643 |
| D | HOH749 |
| D | HOH766 |
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 |
| B | ASP202-SER216 | |
| A | ASP202-SER216 |
