3M1Y
Crystal Structure of a Phosphoserine phosphatase (SerB) from Helicobacter pylori
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006564 | biological_process | L-serine biosynthetic process |
| A | 0008652 | biological_process | amino acid biosynthetic process |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0036424 | molecular_function | L-phosphoserine phosphatase activity |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006564 | biological_process | L-serine biosynthetic process |
| B | 0008652 | biological_process | amino acid biosynthetic process |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0036424 | molecular_function | L-phosphoserine phosphatase activity |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0000287 | molecular_function | magnesium ion binding |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0006564 | biological_process | L-serine biosynthetic process |
| C | 0008652 | biological_process | amino acid biosynthetic process |
| C | 0016787 | molecular_function | hydrolase activity |
| C | 0036424 | molecular_function | L-phosphoserine phosphatase activity |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0000287 | molecular_function | magnesium ion binding |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0006564 | biological_process | L-serine biosynthetic process |
| D | 0008652 | biological_process | amino acid biosynthetic process |
| D | 0016787 | molecular_function | hydrolase activity |
| D | 0036424 | molecular_function | L-phosphoserine phosphatase activity |
| D | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG A 300 |
| Chain | Residue |
| A | ASP8 |
| A | ASP10 |
| A | ASP164 |
| A | HOH319 |
| A | HOH321 |
| A | HOH323 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CL A 302 |
| Chain | Residue |
| A | ASN167 |
| A | HOH323 |
| A | ASP8 |
| A | GLY97 |
| A | LYS141 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL A 303 |
| Chain | Residue |
| A | PHE46 |
| A | HIS47 |
| A | SER138 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG B 300 |
| Chain | Residue |
| B | ASP8 |
| B | ASP10 |
| B | ASP164 |
| B | HOH315 |
| B | HOH316 |
| B | HOH324 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL B 302 |
| Chain | Residue |
| B | GLY97 |
| B | LYS141 |
| B | ASN167 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG C 300 |
| Chain | Residue |
| C | ASP8 |
| C | ASP10 |
| C | ASP164 |
| C | HOH313 |
| C | HOH317 |
| C | HOH326 |
| site_id | AC7 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL C 302 |
| Chain | Residue |
| C | GLY97 |
| C | LYS141 |
| site_id | AC8 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE MG C 301 |
| Chain | Residue |
| C | ASP199 |
| C | HOH312 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG D 300 |
| Chain | Residue |
| D | ASP8 |
| D | ASP10 |
| D | ASP164 |
| D | HOH328 |
| site_id | BC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CL D 302 |
| Chain | Residue |
| D | ASP8 |
| D | GLY97 |
| D | LYS141 |
| D | ASN167 |
| D | HOH327 |
