1I41
CYSTATHIONINE GAMMA-SYNTHASE IN COMPLEX WITH THE INHIBITOR APPA
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 | 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 | 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 | 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 | 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 | 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 | 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 | 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 | 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 | 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 | 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 | 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 | 0019346 | biological_process | transsulfuration |
| L | 0030170 | molecular_function | pyridoxal phosphate binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE HEN A 500 |
| Chain | Residue |
| A | SER137 |
| A | THR260 |
| A | LYS261 |
| A | PRO387 |
| A | SER388 |
| A | SER403 |
| A | ARG423 |
| C | GLU107 |
| C | TYR108 |
| C | ARG110 |
| C | TYR111 |
| A | GLY138 |
| A | MET139 |
| A | TYR163 |
| A | GLU207 |
| A | ASN211 |
| A | ASP236 |
| A | THR238 |
| A | SER258 |
| site_id | AC2 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE HEN B 501 |
| Chain | Residue |
| B | SER137 |
| B | GLY138 |
| B | MET139 |
| B | TYR163 |
| B | GLU207 |
| B | ASN211 |
| B | ASP236 |
| B | THR238 |
| B | SER258 |
| B | THR260 |
| B | LYS261 |
| B | PRO387 |
| B | SER388 |
| B | PHE389 |
| B | SER403 |
| B | ARG423 |
| D | GLU107 |
| D | TYR108 |
| D | ARG110 |
| D | TYR111 |
| site_id | AC3 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE HEN C 502 |
| Chain | Residue |
| A | GLU107 |
| A | TYR108 |
| A | ARG110 |
| A | TYR111 |
| C | SER137 |
| C | GLY138 |
| C | MET139 |
| C | TYR163 |
| C | GLU207 |
| C | ASP236 |
| C | SER258 |
| C | THR260 |
| C | LYS261 |
| C | SER388 |
| C | PHE389 |
| C | SER403 |
| C | ARG423 |
| site_id | AC4 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE HEN D 503 |
| Chain | Residue |
| B | GLU107 |
| B | TYR108 |
| B | ARG110 |
| B | TYR111 |
| D | SER137 |
| D | GLY138 |
| D | MET139 |
| D | TYR163 |
| D | GLU207 |
| D | ASN211 |
| D | ASP236 |
| D | THR238 |
| D | SER258 |
| D | THR260 |
| D | LYS261 |
| D | PRO387 |
| D | SER388 |
| D | PHE389 |
| D | SER403 |
| D | ARG423 |
| site_id | AC5 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE HEN E 504 |
| Chain | Residue |
| E | SER137 |
| E | GLY138 |
| E | MET139 |
| E | TYR163 |
| E | LYS165 |
| E | GLU207 |
| E | ASP236 |
| E | THR238 |
| E | SER258 |
| E | THR260 |
| E | LYS261 |
| E | SER388 |
| E | PHE389 |
| E | SER403 |
| E | ARG423 |
| G | GLU107 |
| G | TYR108 |
| G | ARG110 |
| G | TYR111 |
| site_id | AC6 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE HEN F 505 |
| Chain | Residue |
| F | GLU207 |
| F | ASN211 |
| F | ASP236 |
| F | SER258 |
| F | THR260 |
| F | LYS261 |
| F | SER388 |
| F | PHE389 |
| F | SER403 |
| F | ARG423 |
| H | GLU107 |
| H | TYR108 |
| H | ARG110 |
| H | TYR111 |
| F | SER137 |
| F | GLY138 |
| F | MET139 |
| F | TYR163 |
| site_id | AC7 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE HEN G 506 |
| Chain | Residue |
| E | GLU107 |
| E | TYR108 |
| E | ARG110 |
| E | TYR111 |
| G | SER137 |
| G | GLY138 |
| G | MET139 |
| G | TYR163 |
| G | GLU207 |
| G | ASN211 |
| G | ASP236 |
| G | SER258 |
| G | THR260 |
| G | LYS261 |
| G | PRO387 |
| G | SER388 |
| G | PHE389 |
| G | SER403 |
| G | ARG423 |
| site_id | AC8 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE HEN H 507 |
| Chain | Residue |
| F | GLU107 |
| F | TYR108 |
| F | ARG110 |
| F | TYR111 |
| H | SER137 |
| H | GLY138 |
| H | MET139 |
| H | TYR163 |
| H | GLU207 |
| H | ASN211 |
| H | ASP236 |
| H | THR238 |
| H | SER258 |
| H | THR260 |
| H | LYS261 |
| H | PHE389 |
| H | SER403 |
| H | ARG423 |
| site_id | AC9 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE HEN I 508 |
| Chain | Residue |
| I | SER137 |
| I | GLY138 |
| I | MET139 |
| I | TYR163 |
| I | GLU207 |
| I | ASN211 |
| I | ASP236 |
| I | THR238 |
| I | SER258 |
| I | THR260 |
| I | LYS261 |
| I | PRO387 |
| I | SER388 |
| I | PHE389 |
| I | SER403 |
| I | ARG423 |
| K | GLU107 |
| K | TYR108 |
| K | ARG110 |
| K | TYR111 |
| site_id | BC1 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE HEN J 509 |
| Chain | Residue |
| J | SER137 |
| J | GLY138 |
| J | MET139 |
| J | TYR163 |
| J | GLU207 |
| J | ASP236 |
| J | THR238 |
| J | SER258 |
| J | THR260 |
| J | LYS261 |
| J | SER388 |
| J | PHE389 |
| J | SER403 |
| J | ARG423 |
| L | GLU107 |
| L | TYR108 |
| L | ARG110 |
| L | TYR111 |
| site_id | BC2 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE HEN K 510 |
| Chain | Residue |
| I | GLU107 |
| I | TYR108 |
| I | ARG110 |
| I | TYR111 |
| K | SER137 |
| K | GLY138 |
| K | MET139 |
| K | TYR163 |
| K | LYS165 |
| K | ASP236 |
| K | SER258 |
| K | THR260 |
| K | LYS261 |
| K | SER388 |
| K | PHE389 |
| K | SER403 |
| K | ARG423 |
| site_id | BC3 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE HEN L 511 |
| Chain | Residue |
| J | GLU107 |
| J | TYR108 |
| J | ARG110 |
| J | TYR111 |
| L | SER137 |
| L | GLY138 |
| L | MET139 |
| L | TYR163 |
| L | GLU207 |
| L | ASN211 |
| L | ASP236 |
| L | THR238 |
| L | SER258 |
| L | THR260 |
| L | LYS261 |
| L | SER388 |
| L | PHE389 |
| L | SER403 |
| L | ARG423 |
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 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1b8g |
| Chain | Residue | Details |
| A | ASP236 | |
| A | LYS261 | |
| A | TYR163 |
| site_id | CSA10 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1b8g |
| Chain | Residue | Details |
| J | ASP236 | |
| J | LYS261 | |
| J | TYR163 |
| site_id | CSA11 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1b8g |
| Chain | Residue | Details |
| K | ASP236 | |
| K | LYS261 | |
| K | TYR163 |
| site_id | CSA12 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1b8g |
| Chain | Residue | Details |
| L | ASP236 | |
| L | LYS261 | |
| L | TYR163 |
| site_id | CSA13 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1b8g |
| Chain | Residue | Details |
| A | ARG110 | |
| C | ASP236 | |
| C | TYR163 |
| site_id | CSA14 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1b8g |
| Chain | Residue | Details |
| D | ASP236 | |
| D | TYR163 | |
| B | ARG110 |
| site_id | CSA15 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1b8g |
| Chain | Residue | Details |
| A | ASP236 | |
| A | TYR163 | |
| C | ARG110 |
| site_id | CSA16 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1b8g |
| Chain | Residue | Details |
| D | ARG110 | |
| B | ASP236 | |
| B | TYR163 |
| site_id | CSA17 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1b8g |
| Chain | Residue | Details |
| G | ASP236 | |
| G | TYR163 | |
| E | ARG110 |
| site_id | CSA18 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1b8g |
| Chain | Residue | Details |
| F | ARG110 | |
| H | ASP236 | |
| H | TYR163 |
| site_id | CSA19 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1b8g |
| Chain | Residue | Details |
| G | ARG110 | |
| E | ASP236 | |
| E | TYR163 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1b8g |
| Chain | Residue | Details |
| B | ASP236 | |
| B | LYS261 | |
| B | TYR163 |
| site_id | CSA20 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1b8g |
| Chain | Residue | Details |
| H | ARG110 | |
| F | ASP236 | |
| F | TYR163 |
| site_id | CSA21 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1b8g |
| Chain | Residue | Details |
| I | ARG110 | |
| K | ASP236 | |
| K | TYR163 |
| site_id | CSA22 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1b8g |
| Chain | Residue | Details |
| J | ARG110 | |
| L | ASP236 | |
| L | TYR163 |
| site_id | CSA23 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1b8g |
| Chain | Residue | Details |
| K | ARG110 | |
| I | ASP236 | |
| I | TYR163 |
| site_id | CSA24 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1b8g |
| Chain | Residue | Details |
| J | ASP236 | |
| J | TYR163 | |
| L | ARG110 |
| site_id | CSA3 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1b8g |
| Chain | Residue | Details |
| C | ASP236 | |
| C | LYS261 | |
| C | TYR163 |
| site_id | CSA4 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1b8g |
| Chain | Residue | Details |
| D | ASP236 | |
| D | LYS261 | |
| D | TYR163 |
| site_id | CSA5 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1b8g |
| Chain | Residue | Details |
| E | ASP236 | |
| E | LYS261 | |
| E | TYR163 |
| site_id | CSA6 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1b8g |
| Chain | Residue | Details |
| F | ASP236 | |
| F | LYS261 | |
| F | TYR163 |
| site_id | CSA7 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1b8g |
| Chain | Residue | Details |
| G | ASP236 | |
| G | LYS261 | |
| G | TYR163 |
| site_id | CSA8 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1b8g |
| Chain | Residue | Details |
| H | ASP236 | |
| H | LYS261 | |
| H | TYR163 |
| site_id | CSA9 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1b8g |
| Chain | Residue | Details |
| I | ASP236 | |
| I | LYS261 | |
| I | TYR163 |
