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 | 0004123 | molecular_function | cystathionine gamma-lyase activity |
A | 0005737 | cellular_component | cytoplasm |
A | 0009086 | biological_process | methionine biosynthetic process |
A | 0019343 | biological_process | cysteine biosynthetic process via cystathionine |
A | 0019346 | biological_process | transsulfuration |
A | 0030170 | molecular_function | pyridoxal phosphate binding |
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 | 0019343 | biological_process | cysteine biosynthetic process via cystathionine |
B | 0019346 | biological_process | transsulfuration |
B | 0030170 | molecular_function | pyridoxal phosphate binding |
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 | 0019343 | biological_process | cysteine biosynthetic process via cystathionine |
C | 0019346 | biological_process | transsulfuration |
C | 0030170 | molecular_function | pyridoxal phosphate binding |
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 | 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 | 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 |