1N8P
Crystal Structure of cystathionine gamma-lyase from yeast
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004123 | molecular_function | cystathionine gamma-lyase activity |
| A | 0005634 | cellular_component | nucleus |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0016829 | molecular_function | lyase activity |
| A | 0019343 | biological_process | cysteine biosynthetic process via cystathionine |
| A | 0019344 | biological_process | cysteine biosynthetic process |
| A | 0019346 | biological_process | transsulfuration |
| A | 0030170 | molecular_function | pyridoxal phosphate binding |
| A | 0044540 | molecular_function | L-cystine L-cysteine-lyase (deaminating) |
| A | 0047804 | molecular_function | cysteine-S-conjugate beta-lyase activity |
| A | 0080146 | molecular_function | L-cysteine desulfhydrase activity |
| A | 1904828 | biological_process | positive regulation of hydrogen sulfide biosynthetic process |
| B | 0004123 | molecular_function | cystathionine gamma-lyase activity |
| B | 0005634 | cellular_component | nucleus |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0016829 | molecular_function | lyase activity |
| B | 0019343 | biological_process | cysteine biosynthetic process via cystathionine |
| B | 0019344 | biological_process | cysteine biosynthetic process |
| B | 0019346 | biological_process | transsulfuration |
| B | 0030170 | molecular_function | pyridoxal phosphate binding |
| B | 0044540 | molecular_function | L-cystine L-cysteine-lyase (deaminating) |
| B | 0047804 | molecular_function | cysteine-S-conjugate beta-lyase activity |
| B | 0080146 | molecular_function | L-cysteine desulfhydrase activity |
| B | 1904828 | biological_process | positive regulation of hydrogen sulfide biosynthetic process |
| C | 0004123 | molecular_function | cystathionine gamma-lyase activity |
| C | 0005634 | cellular_component | nucleus |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0016829 | molecular_function | lyase activity |
| C | 0019343 | biological_process | cysteine biosynthetic process via cystathionine |
| C | 0019344 | biological_process | cysteine biosynthetic process |
| C | 0019346 | biological_process | transsulfuration |
| C | 0030170 | molecular_function | pyridoxal phosphate binding |
| C | 0044540 | molecular_function | L-cystine L-cysteine-lyase (deaminating) |
| C | 0047804 | molecular_function | cysteine-S-conjugate beta-lyase activity |
| C | 0080146 | molecular_function | L-cysteine desulfhydrase activity |
| C | 1904828 | biological_process | positive regulation of hydrogen sulfide biosynthetic process |
| D | 0004123 | molecular_function | cystathionine gamma-lyase activity |
| D | 0005634 | cellular_component | nucleus |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0016829 | molecular_function | lyase activity |
| D | 0019343 | biological_process | cysteine biosynthetic process via cystathionine |
| D | 0019344 | biological_process | cysteine biosynthetic process |
| D | 0019346 | biological_process | transsulfuration |
| D | 0030170 | molecular_function | pyridoxal phosphate binding |
| D | 0044540 | molecular_function | L-cystine L-cysteine-lyase (deaminating) |
| D | 0047804 | molecular_function | cysteine-S-conjugate beta-lyase activity |
| D | 0080146 | molecular_function | L-cysteine desulfhydrase activity |
| D | 1904828 | biological_process | positive regulation of hydrogen sulfide biosynthetic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE PLP A 400 |
| Chain | Residue |
| A | SER78 |
| A | VAL212 |
| B | TYR49 |
| B | ARG51 |
| A | GLY79 |
| A | SER80 |
| A | TYR103 |
| A | ASP178 |
| A | PHE181 |
| A | SER200 |
| A | THR202 |
| A | LYS203 |
| site_id | AC2 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE PLP B 400 |
| Chain | Residue |
| A | TYR49 |
| A | ARG51 |
| B | SER78 |
| B | GLY79 |
| B | SER80 |
| B | TYR103 |
| B | ASP178 |
| B | THR180 |
| B | PHE181 |
| B | SER200 |
| B | THR202 |
| B | LYS203 |
| B | HOH409 |
| site_id | AC3 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE PLP C 400 |
| Chain | Residue |
| C | SER78 |
| C | GLY79 |
| C | SER80 |
| C | TYR103 |
| C | ASP178 |
| C | PHE181 |
| C | SER200 |
| C | THR202 |
| C | LYS203 |
| D | TYR49 |
| D | ARG51 |
| site_id | AC4 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE PLP D 400 |
| Chain | Residue |
| C | TYR49 |
| D | SER78 |
| D | GLY79 |
| D | SER80 |
| D | TYR103 |
| D | GLU145 |
| D | ASP178 |
| D | PHE181 |
| D | SER200 |
| D | LYS203 |
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. DIvvhSATKYInGHS |
| Chain | Residue | Details |
| A | ASP195-SER209 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 16 |
| Details | BINDING: BINDING => ECO:0000250 |
| Chain | Residue | Details |
| A | SER52 | |
| C | GLY104 | |
| C | TYR109 | |
| C | SER334 | |
| D | SER52 | |
| D | GLY104 | |
| D | TYR109 | |
| D | SER334 | |
| A | GLY104 | |
| A | TYR109 | |
| A | SER334 | |
| B | SER52 | |
| B | GLY104 | |
| B | TYR109 | |
| B | SER334 | |
| C | SER52 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | MOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000250 |
| Chain | Residue | Details |
| A | TYR204 | |
| B | TYR204 | |
| C | TYR204 | |
| D | TYR204 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198 |
| Chain | Residue | Details |
| A | GLY362 | |
| B | GLY362 | |
| C | GLY362 | |
| D | GLY362 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1b8g |
| Chain | Residue | Details |
| A | TYR103 | |
| A | LYS203 | |
| A | ASP178 |
| site_id | CSA10 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1b8g |
| Chain | Residue | Details |
| A | TYR103 | |
| A | ASP178 | |
| B | ARG51 |
| site_id | CSA11 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1b8g |
| Chain | Residue | Details |
| C | ARG51 | |
| D | TYR103 | |
| D | ASP178 |
| site_id | CSA12 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1b8g |
| Chain | Residue | Details |
| D | ARG51 | |
| C | TYR103 | |
| C | ASP178 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1b8g |
| Chain | Residue | Details |
| B | TYR103 | |
| B | LYS203 | |
| B | ASP178 |
| site_id | CSA3 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1b8g |
| Chain | Residue | Details |
| C | TYR103 | |
| C | LYS203 | |
| C | ASP178 |
| site_id | CSA4 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1b8g |
| Chain | Residue | Details |
| D | TYR103 | |
| D | LYS203 | |
| D | ASP178 |
| site_id | CSA5 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1b8g |
| Chain | Residue | Details |
| A | PHE110 | |
| A | LYS203 | |
| A | ASP178 |
| site_id | CSA6 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1b8g |
| Chain | Residue | Details |
| B | PHE110 | |
| B | LYS203 | |
| B | ASP178 |
| site_id | CSA7 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1b8g |
| Chain | Residue | Details |
| C | PHE110 | |
| C | LYS203 | |
| C | ASP178 |
| site_id | CSA8 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1b8g |
| Chain | Residue | Details |
| D | PHE110 | |
| D | LYS203 | |
| D | ASP178 |
| site_id | CSA9 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1b8g |
| Chain | Residue | Details |
| A | ARG51 | |
| B | TYR103 | |
| B | ASP178 |
