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 | 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 | 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 | 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 | 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 |