2PK0
Structure of the S. agalactiae serine/threonine phosphatase at 2.65 resolution
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004722 | molecular_function | protein serine/threonine phosphatase activity |
A | 0006470 | biological_process | protein dephosphorylation |
A | 0016787 | molecular_function | hydrolase activity |
A | 0016791 | molecular_function | phosphatase activity |
A | 0017018 | molecular_function | myosin phosphatase activity |
A | 0046872 | molecular_function | metal ion binding |
B | 0004722 | molecular_function | protein serine/threonine phosphatase activity |
B | 0006470 | biological_process | protein dephosphorylation |
B | 0016787 | molecular_function | hydrolase activity |
B | 0016791 | molecular_function | phosphatase activity |
B | 0017018 | molecular_function | myosin phosphatase activity |
B | 0046872 | molecular_function | metal ion binding |
C | 0004722 | molecular_function | protein serine/threonine phosphatase activity |
C | 0006470 | biological_process | protein dephosphorylation |
C | 0016787 | molecular_function | hydrolase activity |
C | 0016791 | molecular_function | phosphatase activity |
C | 0017018 | molecular_function | myosin phosphatase activity |
C | 0046872 | molecular_function | metal ion binding |
D | 0004722 | molecular_function | protein serine/threonine phosphatase activity |
D | 0006470 | biological_process | protein dephosphorylation |
D | 0016787 | molecular_function | hydrolase activity |
D | 0016791 | molecular_function | phosphatase activity |
D | 0017018 | molecular_function | myosin 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 501 |
Chain | Residue |
A | ASP36 |
A | GLY37 |
A | HOH578 |
A | HOH579 |
A | HOH580 |
A | HOH583 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG A 502 |
Chain | Residue |
A | HOH581 |
A | HOH582 |
A | HOH583 |
A | ASP36 |
A | ASP192 |
A | ASP231 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG B 503 |
Chain | Residue |
B | ASP36 |
B | GLY37 |
B | HOH609 |
B | HOH680 |
B | HOH684 |
B | HOH685 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG B 510 |
Chain | Residue |
B | ASP36 |
B | ASP192 |
B | ASP231 |
B | HOH681 |
B | HOH682 |
B | HOH685 |
site_id | AC5 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE MG C 504 |
Chain | Residue |
C | ASP36 |
C | GLY37 |
C | MG508 |
C | HOH560 |
C | HOH561 |
C | HOH562 |
C | HOH565 |
site_id | AC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG C 505 |
Chain | Residue |
C | ASP118 |
C | ASP192 |
C | HOH563 |
C | HOH566 |
C | HOH567 |
C | HOH568 |
site_id | AC7 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE MG C 508 |
Chain | Residue |
C | ASP36 |
C | ASP192 |
C | ASP231 |
C | MG504 |
C | HOH564 |
C | HOH565 |
C | HOH569 |
site_id | AC8 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG D 506 |
Chain | Residue |
D | ASP36 |
D | GLY37 |
D | HOH758 |
D | HOH759 |
D | HOH760 |
D | HOH765 |
site_id | AC9 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG D 507 |
Chain | Residue |
D | ASP36 |
D | ASP192 |
D | ASP231 |
D | HOH760 |
D | HOH762 |
D | HOH763 |
site_id | BC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG D 509 |
Chain | Residue |
D | ASP118 |
D | ASP192 |
D | HOH727 |
D | HOH728 |
D | HOH761 |
D | HOH766 |
site_id | BC2 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE CL D 701 |
Chain | Residue |
D | HIS179 |
site_id | BC3 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE GOL B 601 |
Chain | Residue |
B | TYR0 |
B | GLU241 |