1CS1
CYSTATHIONINE GAMMA-SYNTHASE (CGS) FROM ESCHERICHIA COLI
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0003962 | molecular_function | cystathionine gamma-synthase activity |
| A | 0004123 | molecular_function | cystathionine gamma-lyase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0009086 | biological_process | methionine biosynthetic process |
| A | 0016740 | molecular_function | transferase activity |
| A | 0019343 | biological_process | cysteine biosynthetic process via cystathionine |
| A | 0019346 | biological_process | transsulfuration |
| A | 0030170 | molecular_function | pyridoxal phosphate binding |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0003962 | molecular_function | cystathionine gamma-synthase activity |
| B | 0004123 | molecular_function | cystathionine gamma-lyase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0009086 | biological_process | methionine biosynthetic process |
| B | 0016740 | molecular_function | transferase activity |
| B | 0019343 | biological_process | cysteine biosynthetic process via cystathionine |
| B | 0019346 | biological_process | transsulfuration |
| B | 0030170 | molecular_function | pyridoxal phosphate binding |
| C | 0003824 | molecular_function | catalytic activity |
| C | 0003962 | molecular_function | cystathionine gamma-synthase activity |
| C | 0004123 | molecular_function | cystathionine gamma-lyase activity |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0009086 | biological_process | methionine biosynthetic process |
| C | 0016740 | molecular_function | transferase activity |
| C | 0019343 | biological_process | cysteine biosynthetic process via cystathionine |
| C | 0019346 | biological_process | transsulfuration |
| C | 0030170 | molecular_function | pyridoxal phosphate binding |
| D | 0003824 | molecular_function | catalytic activity |
| D | 0003962 | molecular_function | cystathionine gamma-synthase activity |
| D | 0004123 | molecular_function | cystathionine gamma-lyase activity |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0009086 | biological_process | methionine biosynthetic process |
| D | 0016740 | molecular_function | transferase 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 | 8 |
| Details | BINDING SITE FOR RESIDUE DHD D 1501 |
| Chain | Residue |
| D | HOH1654 |
| D | HOH1664 |
| D | HOH1664 |
| D | ALA157 |
| D | ALA157 |
| D | LYS158 |
| D | LYS158 |
| D | HIS161 |
| site_id | PLA |
| Number of Residues | 1 |
| Details | COFACTOR SITE CHAIN A |
| Chain | Residue |
| A | LLP198 |
| site_id | PLB |
| Number of Residues | 1 |
| Details | COFACTOR SITE CHAIN B |
| Chain | Residue |
| B | LLP198 |
| site_id | PLC |
| Number of Residues | 1 |
| Details | COFACTOR SITE CHAIN C |
| Chain | Residue |
| C | LLP198 |
| site_id | PLD |
| Number of Residues | 1 |
| Details | COFACTOR SITE CHAIN D |
| Chain | Residue |
| D | LLP198 |
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. DLvlhSCTKYLnGHS |
| Chain | Residue | Details |
| A | ASP190-SER204 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | MOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:3307782 |
| Chain | Residue | Details |
| A | LLP198 | |
| B | LLP198 | |
| C | LLP198 | |
| D | LLP198 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 4 |
| Details | a catalytic site defined by CSA, PubMed 9843488, 8831789, 14503880 |
| Chain | Residue | Details |
| A | LLP198 | |
| A | TYR101 | |
| A | ASP173 | |
| C | ARG48 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | a catalytic site defined by CSA, PubMed 9843488, 8831789, 14503880 |
| Chain | Residue | Details |
| A | ARG48 | |
| C | ASP173 | |
| C | TYR101 |
| site_id | CSA3 |
| Number of Residues | 3 |
| Details | a catalytic site defined by CSA, PubMed 9843488, 8831789, 14503880 |
| Chain | Residue | Details |
| D | ASP173 | |
| D | TYR101 | |
| B | ARG48 |
| site_id | CSA4 |
| Number of Residues | 3 |
| Details | a catalytic site defined by CSA, PubMed 9843488, 8831789, 14503880 |
| Chain | Residue | Details |
| D | ARG48 | |
| B | TYR101 | |
| B | ASP173 |
| site_id | MCSA1 |
| Number of Residues | 4 |
| Details | M-CSA 759 |
| Chain | Residue | Details |
| A | ARG48 | electrostatic stabiliser |
| A | TYR101 | electrostatic stabiliser, proton acceptor, proton donor |
| A | ASP173 | electrostatic stabiliser |
| A | LLP198 | covalently attached, electron pair acceptor, electron pair donor, electrostatic stabiliser, nucleofuge, nucleophile, proton acceptor, proton donor |
| site_id | MCSA2 |
| Number of Residues | 4 |
| Details | M-CSA 759 |
| Chain | Residue | Details |
| B | ARG48 | electrostatic stabiliser |
| B | TYR101 | electrostatic stabiliser, proton acceptor, proton donor |
| B | ASP173 | electrostatic stabiliser |
| B | LLP198 | covalently attached, electron pair acceptor, electron pair donor, electrostatic stabiliser, nucleofuge, nucleophile, proton acceptor, proton donor |
| site_id | MCSA3 |
| Number of Residues | 4 |
| Details | M-CSA 759 |
| Chain | Residue | Details |
| C | ARG48 | electrostatic stabiliser |
| C | TYR101 | electrostatic stabiliser, proton acceptor, proton donor |
| C | ASP173 | electrostatic stabiliser |
| C | LLP198 | covalently attached, electron pair acceptor, electron pair donor, electrostatic stabiliser, nucleofuge, nucleophile, proton acceptor, proton donor |
| site_id | MCSA4 |
| Number of Residues | 4 |
| Details | M-CSA 759 |
| Chain | Residue | Details |
| D | ARG48 | electrostatic stabiliser |
| D | TYR101 | electrostatic stabiliser, proton acceptor, proton donor |
| D | ASP173 | electrostatic stabiliser |
| D | LLP198 | covalently attached, electron pair acceptor, electron pair donor, electrostatic stabiliser, nucleofuge, nucleophile, proton acceptor, proton donor |
