2FEA
Crystal structure of MtnX phosphatase from Bacillus Subtilis at 2.00 A resolution
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0008253 | molecular_function | 5'-nucleotidase activity |
| A | 0008652 | biological_process | amino acid biosynthetic process |
| A | 0009086 | biological_process | methionine biosynthetic process |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0016791 | molecular_function | phosphatase activity |
| A | 0019509 | biological_process | L-methionine salvage from methylthioadenosine |
| A | 0043716 | molecular_function | 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate phosphatase activity |
| A | 0071267 | biological_process | L-methionine salvage |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0008253 | molecular_function | 5'-nucleotidase activity |
| B | 0008652 | biological_process | amino acid biosynthetic process |
| B | 0009086 | biological_process | methionine biosynthetic process |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0016791 | molecular_function | phosphatase activity |
| B | 0019509 | biological_process | L-methionine salvage from methylthioadenosine |
| B | 0043716 | molecular_function | 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate phosphatase activity |
| B | 0071267 | biological_process | L-methionine salvage |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG A 1301 |
| Chain | Residue |
| A | ASP11 |
| A | ASP13 |
| A | ASP170 |
| A | SER171 |
| A | HOH1453 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 1302 |
| Chain | Residue |
| A | CYS139 |
| A | CYS143 |
| A | CYS147 |
| A | CYS150 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG B 2301 |
| Chain | Residue |
| B | ASP11 |
| B | ASP13 |
| B | ASP170 |
| B | HOH2322 |
| B | HOH2354 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 2302 |
| Chain | Residue |
| B | CYS139 |
| B | CYS143 |
| B | CYS147 |
| B | CYS150 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO A 1303 |
| Chain | Residue |
| A | HIS137 |
| A | SER138 |
| A | LYS140 |
| A | SER153 |
| A | HOH1340 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO A 1304 |
| Chain | Residue |
| A | LYS116 |
| A | ASP117 |
| A | ILE119 |
| A | TYR120 |
| A | HIS137 |
| A | HOH1407 |
| A | HOH1452 |
| site_id | AC7 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE EDO A 1305 |
| Chain | Residue |
| A | THR17 |
| A | MSE18 |
| A | ASN19 |
| A | ASN21 |
| A | ASN24 |
| A | ASP74 |
| A | ALA75 |
| A | LYS76 |
| site_id | AC8 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE EDO A 1306 |
| Chain | Residue |
| A | ASP20 |
| site_id | AC9 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO B 2303 |
| Chain | Residue |
| B | PRO60 |
| B | SER62 |
| B | HOH2415 |
| site_id | BC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO B 2304 |
| Chain | Residue |
| B | ASP117 |
| B | ILE119 |
| B | HIS137 |
| site_id | BC2 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE EDO B 2305 |
| Chain | Residue |
| B | ASP20 |
| B | LYS38 |
| site_id | BC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO B 2306 |
| Chain | Residue |
| B | GLU115 |
| B | ASP117 |
| B | ARG118 |
| site_id | BC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO B 2307 |
| Chain | Residue |
| A | ARG54 |
| A | HOH1331 |
| B | PRO32 |
| B | GLU33 |
| B | ALA36 |
| B | HOH2398 |
| site_id | BC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO B 2308 |
| Chain | Residue |
| B | HIS137 |
| B | SER138 |
| B | LYS140 |
| B | SER153 |
| B | GLU157 |
| B | HOH2450 |
| B | HOH2454 |
