3QHX
Crystal Structure of Cystathionine gamma-synthase MetB (Cgs) from Mycobacterium ulcerans Agy99 bound to HEPES
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003962 | molecular_function | cystathionine gamma-synthase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0009086 | biological_process | methionine biosynthetic process |
| A | 0016846 | molecular_function | carbon-sulfur lyase activity |
| A | 0019346 | biological_process | transsulfuration |
| A | 0030170 | molecular_function | pyridoxal phosphate binding |
| B | 0003962 | molecular_function | cystathionine gamma-synthase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0009086 | biological_process | methionine biosynthetic process |
| B | 0016846 | molecular_function | carbon-sulfur lyase activity |
| B | 0019346 | biological_process | transsulfuration |
| B | 0030170 | molecular_function | pyridoxal phosphate binding |
| C | 0003962 | molecular_function | cystathionine gamma-synthase activity |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0009086 | biological_process | methionine biosynthetic process |
| C | 0016846 | molecular_function | carbon-sulfur lyase activity |
| C | 0019346 | biological_process | transsulfuration |
| C | 0030170 | molecular_function | pyridoxal phosphate binding |
| D | 0003962 | molecular_function | cystathionine gamma-synthase activity |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0009086 | biological_process | methionine biosynthetic process |
| D | 0016846 | molecular_function | carbon-sulfur lyase activity |
| D | 0019346 | biological_process | transsulfuration |
| D | 0030170 | molecular_function | pyridoxal phosphate binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 A 389 |
| Chain | Residue |
| A | ARG116 |
| A | LYS120 |
| A | HIS352 |
| A | ALA353 |
| A | SER354 |
| site_id | AC2 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE EPE A 390 |
| Chain | Residue |
| A | SER336 |
| A | MET350 |
| A | ARG368 |
| B | GLU55 |
| B | TYR56 |
| B | ARG58 |
| B | THR59 |
| B | SO4389 |
| A | TYR111 |
| A | ASN158 |
| A | LLP208 |
| A | GLU335 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL A 391 |
| Chain | Residue |
| A | ARG95 |
| A | PHE122 |
| A | TRP125 |
| B | ARG95 |
| B | PHE122 |
| B | TRP125 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SO4 B 389 |
| Chain | Residue |
| A | ARG116 |
| A | HIS352 |
| A | EPE390 |
| B | ASN237 |
| B | HOH918 |
| B | HOH1610 |
| B | HOH2003 |
| B | HOH2015 |
| site_id | AC5 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE SO4 B 390 |
| Chain | Residue |
| B | TYR111 |
| B | ASN158 |
| B | LLP208 |
| B | GLU335 |
| B | SER336 |
| B | LEU337 |
| B | GLU345 |
| B | ARG368 |
| B | HOH2212 |
| site_id | AC6 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE SO4 B 391 |
| Chain | Residue |
| B | ARG313 |
| site_id | AC7 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 C 389 |
| Chain | Residue |
| C | TYR111 |
| C | ASN158 |
| C | LLP208 |
| C | SER336 |
| C | LEU337 |
| C | GLU345 |
| C | ARG368 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NA C 390 |
| Chain | Residue |
| C | VAL216 |
| C | VAL217 |
| C | ASP247 |
| C | HOH2089 |
| C | HOH2537 |
| D | PRO245 |
| site_id | AC9 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SO4 D 389 |
| Chain | Residue |
| D | TYR111 |
| D | ASN158 |
| D | LLP208 |
| D | SER336 |
| D | GLU345 |
| D | ARG368 |
| D | HOH1257 |
| D | HOH2224 |
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. DVvlhSTTKYIgGHS |
| Chain | Residue | Details |
| A | ASP200-SER214 |
