1I48
CYSTATHIONINE GAMMA-SYNTHASE IN COMPLEX WITH THE INHIBITOR CTCPO
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003962 | molecular_function | cystathionine gamma-synthase activity |
| A | 0009086 | biological_process | methionine biosynthetic process |
| A | 0009507 | cellular_component | chloroplast |
| A | 0019346 | biological_process | transsulfuration |
| A | 0030170 | molecular_function | pyridoxal phosphate binding |
| B | 0003962 | molecular_function | cystathionine gamma-synthase activity |
| B | 0009086 | biological_process | methionine biosynthetic process |
| B | 0009507 | cellular_component | chloroplast |
| B | 0019346 | biological_process | transsulfuration |
| B | 0030170 | molecular_function | pyridoxal phosphate binding |
| C | 0003962 | molecular_function | cystathionine gamma-synthase activity |
| C | 0009086 | biological_process | methionine biosynthetic process |
| C | 0009507 | cellular_component | chloroplast |
| C | 0019346 | biological_process | transsulfuration |
| C | 0030170 | molecular_function | pyridoxal phosphate binding |
| D | 0003962 | molecular_function | cystathionine gamma-synthase activity |
| D | 0009086 | biological_process | methionine biosynthetic process |
| D | 0009507 | cellular_component | chloroplast |
| D | 0019346 | biological_process | transsulfuration |
| D | 0030170 | molecular_function | pyridoxal phosphate binding |
| E | 0003962 | molecular_function | cystathionine gamma-synthase activity |
| E | 0009086 | biological_process | methionine biosynthetic process |
| E | 0009507 | cellular_component | chloroplast |
| E | 0019346 | biological_process | transsulfuration |
| E | 0030170 | molecular_function | pyridoxal phosphate binding |
| F | 0003962 | molecular_function | cystathionine gamma-synthase activity |
| F | 0009086 | biological_process | methionine biosynthetic process |
| F | 0009507 | cellular_component | chloroplast |
| F | 0019346 | biological_process | transsulfuration |
| F | 0030170 | molecular_function | pyridoxal phosphate binding |
| G | 0003962 | molecular_function | cystathionine gamma-synthase activity |
| G | 0009086 | biological_process | methionine biosynthetic process |
| G | 0009507 | cellular_component | chloroplast |
| G | 0019346 | biological_process | transsulfuration |
| G | 0030170 | molecular_function | pyridoxal phosphate binding |
| H | 0003962 | molecular_function | cystathionine gamma-synthase activity |
| H | 0009086 | biological_process | methionine biosynthetic process |
| H | 0009507 | cellular_component | chloroplast |
| H | 0019346 | biological_process | transsulfuration |
| H | 0030170 | molecular_function | pyridoxal phosphate binding |
| I | 0003962 | molecular_function | cystathionine gamma-synthase activity |
| I | 0009086 | biological_process | methionine biosynthetic process |
| I | 0009507 | cellular_component | chloroplast |
| I | 0019346 | biological_process | transsulfuration |
| I | 0030170 | molecular_function | pyridoxal phosphate binding |
| J | 0003962 | molecular_function | cystathionine gamma-synthase activity |
| J | 0009086 | biological_process | methionine biosynthetic process |
| J | 0009507 | cellular_component | chloroplast |
| J | 0019346 | biological_process | transsulfuration |
| J | 0030170 | molecular_function | pyridoxal phosphate binding |
| K | 0003962 | molecular_function | cystathionine gamma-synthase activity |
| K | 0009086 | biological_process | methionine biosynthetic process |
| K | 0009507 | cellular_component | chloroplast |
| K | 0019346 | biological_process | transsulfuration |
| K | 0030170 | molecular_function | pyridoxal phosphate binding |
| L | 0003962 | molecular_function | cystathionine gamma-synthase activity |
| L | 0009086 | biological_process | methionine biosynthetic process |
| L | 0009507 | cellular_component | chloroplast |
| L | 0019346 | biological_process | transsulfuration |
| L | 0030170 | molecular_function | pyridoxal phosphate binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE PLP A 500 |
| Chain | Residue |
| A | SER137 |
| A | PHE389 |
| C | TYR108 |
| C | ARG110 |
| A | GLY138 |
| A | MET139 |
| A | TYR163 |
| A | GLU207 |
| A | ASP236 |
| A | SER258 |
| A | THR260 |
| A | LYS261 |
| site_id | AC2 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE PLP B 500 |
| Chain | Residue |
| B | SER137 |
| B | GLY138 |
| B | MET139 |
| B | TYR163 |
| B | ASP236 |
| B | THR238 |
| B | SER258 |
| B | THR260 |
| B | LYS261 |
| B | PHE389 |
| D | TYR108 |
| D | ARG110 |
| site_id | AC3 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE PLP C 500 |
| Chain | Residue |
| A | TYR108 |
| A | ARG110 |
| C | SER137 |
| C | GLY138 |
| C | MET139 |
| C | TYR163 |
| C | GLU207 |
| C | ASP236 |
| C | SER258 |
| C | THR260 |
| C | LYS261 |
| C | PHE389 |
| site_id | AC4 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE PLP D 500 |
| Chain | Residue |
| B | TYR108 |
| B | ARG110 |
| D | SER137 |
| D | GLY138 |
| D | MET139 |
| D | TYR163 |
| D | GLU207 |
| D | ASP236 |
| D | SER258 |
| D | THR260 |
| D | LYS261 |
| D | PHE389 |
| site_id | AC5 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE PLP E 500 |
| Chain | Residue |
| E | SER137 |
| E | GLY138 |
| E | MET139 |
| E | TYR163 |
| E | GLU207 |
| E | ASP236 |
| E | THR238 |
| E | SER258 |
| E | THR260 |
| E | LYS261 |
| E | PHE389 |
| G | TYR108 |
| G | ARG110 |
| site_id | AC6 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE PLP F 500 |
| Chain | Residue |
| F | SER137 |
| F | GLY138 |
| F | MET139 |
| F | TYR163 |
| F | GLU207 |
| F | ASP236 |
| F | THR238 |
| F | SER258 |
| F | THR260 |
| F | LYS261 |
| F | PHE389 |
| H | TYR108 |
| H | ARG110 |
| site_id | AC7 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE PLP G 500 |
| Chain | Residue |
| E | TYR108 |
| E | ARG110 |
| G | SER137 |
| G | GLY138 |
| G | MET139 |
| G | TYR163 |
| G | GLU207 |
| G | ASP236 |
| G | SER258 |
| G | THR260 |
| G | LYS261 |
| G | PHE389 |
| site_id | AC8 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE PLP H 500 |
| Chain | Residue |
| F | TYR108 |
| F | ARG110 |
| H | SER137 |
| H | GLY138 |
| H | MET139 |
| H | TYR163 |
| H | GLU207 |
| H | ASP236 |
| H | SER258 |
| H | THR260 |
| H | LYS261 |
| H | PHE389 |
| site_id | AC9 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE PLP I 500 |
| Chain | Residue |
| I | GLY138 |
| I | MET139 |
| I | TYR163 |
| I | GLU207 |
| I | ASP236 |
| I | SER258 |
| I | THR260 |
| I | LYS261 |
| I | PHE389 |
| K | TYR108 |
| K | ARG110 |
| I | SER137 |
| site_id | BC1 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE PLP J 500 |
| Chain | Residue |
| J | SER137 |
| J | GLY138 |
| J | MET139 |
| J | TYR163 |
| J | ASP236 |
| J | THR238 |
| J | SER258 |
| J | THR260 |
| J | LYS261 |
| J | PHE389 |
| L | TYR108 |
| L | ARG110 |
| site_id | BC2 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE PLP K 500 |
| Chain | Residue |
| I | TYR108 |
| I | ARG110 |
| K | SER137 |
| K | GLY138 |
| K | MET139 |
| K | TYR163 |
| K | GLU207 |
| K | ASP236 |
| K | SER258 |
| K | THR260 |
| K | LYS261 |
| K | PHE389 |
| site_id | BC3 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE PLP L 500 |
| Chain | Residue |
| J | TYR108 |
| J | ARG110 |
| L | SER137 |
| L | GLY138 |
| L | MET139 |
| L | TYR163 |
| L | ASP236 |
| L | SER258 |
| L | THR260 |
| L | LYS261 |
| L | PHE389 |
| site_id | BC4 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE CCO A 600 |
| Chain | Residue |
| A | TYR163 |
| A | ARG164 |
| A | ALA386 |
| A | SER388 |
| A | PHE389 |
| A | ASP397 |
| A | SER403 |
| A | TYR404 |
| A | ARG423 |
| A | SER425 |
| site_id | BC5 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE CCO B 601 |
| Chain | Residue |
| B | TYR163 |
| B | ASN211 |
| B | ALA361 |
| B | ALA386 |
| B | SER388 |
| B | PHE389 |
| B | ASP397 |
| B | SER403 |
| B | TYR404 |
| B | ARG423 |
| site_id | BC6 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE CCO C 602 |
| Chain | Residue |
| C | TYR163 |
| C | ARG164 |
| C | ALA386 |
| C | SER388 |
| C | PHE389 |
| C | ASP397 |
| C | SER403 |
| C | TYR404 |
| C | ARG423 |
| C | SER425 |
| site_id | BC7 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE CCO D 603 |
| Chain | Residue |
| D | TYR163 |
| D | ARG164 |
| D | ALA386 |
| D | PRO387 |
| D | SER388 |
| D | PHE389 |
| D | ASP397 |
| D | SER403 |
| D | TYR404 |
| D | ARG423 |
| D | PHE424 |
| D | SER425 |
| site_id | BC8 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE CCO E 604 |
| Chain | Residue |
| E | TYR163 |
| E | ARG164 |
| E | ALA361 |
| E | ALA386 |
| E | SER388 |
| E | PHE389 |
| E | ASP397 |
| E | SER403 |
| E | TYR404 |
| E | ARG423 |
| E | SER425 |
| site_id | BC9 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE CCO F 605 |
| Chain | Residue |
| F | TYR163 |
| F | ARG164 |
| F | ALA386 |
| F | PRO387 |
| F | SER388 |
| F | PHE389 |
| F | ASP397 |
| F | SER403 |
| F | TYR404 |
| F | ARG423 |
| F | SER425 |
| site_id | CC1 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE CCO G 606 |
| Chain | Residue |
| G | TYR163 |
| G | ARG164 |
| G | ALA361 |
| G | SER388 |
| G | PHE389 |
| G | SER403 |
| G | TYR404 |
| G | ARG423 |
| site_id | CC2 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE CCO H 607 |
| Chain | Residue |
| H | TYR163 |
| H | ASN211 |
| H | ALA361 |
| H | ALA386 |
| H | SER388 |
| H | PHE389 |
| H | ASP397 |
| H | SER403 |
| H | TYR404 |
| H | ARG423 |
| H | SER425 |
| site_id | CC3 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE CCO I 608 |
| Chain | Residue |
| I | TYR163 |
| I | ARG164 |
| I | ALA361 |
| I | ALA386 |
| I | PRO387 |
| I | SER388 |
| I | PHE389 |
| I | ASP397 |
| I | SER403 |
| I | ARG423 |
| I | SER425 |
| site_id | CC4 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE CCO J 609 |
| Chain | Residue |
| J | TYR163 |
| J | ARG164 |
| J | ALA386 |
| J | PRO387 |
| J | SER388 |
| J | PHE389 |
| J | ASP397 |
| J | SER403 |
| J | ARG423 |
| site_id | CC5 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE CCO K 610 |
| Chain | Residue |
| K | TYR163 |
| K | ARG164 |
| K | ASN211 |
| K | ALA386 |
| K | PRO387 |
| K | SER388 |
| K | PHE389 |
| K | ASP397 |
| K | SER403 |
| K | TYR404 |
| K | ARG423 |
| site_id | CC6 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE CCO L 611 |
| Chain | Residue |
| L | TYR163 |
| L | ARG164 |
| L | ALA361 |
| L | ALA386 |
| L | SER388 |
| L | PHE389 |
| L | ASP397 |
| L | SER403 |
| L | ARG423 |
| L | SER425 |
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. DLvlhSATKFLgGHN |
| Chain | Residue | Details |
| A | ASP253-ASN267 |
