5OKN
Crystal structure of human SHIP2 Phosphatase-C2 D607A mutant
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0016791 | molecular_function | phosphatase activity |
A | 0046856 | biological_process | phosphatidylinositol dephosphorylation |
B | 0016791 | molecular_function | phosphatase activity |
B | 0046856 | biological_process | phosphatidylinositol dephosphorylation |
C | 0016791 | molecular_function | phosphatase activity |
C | 0046856 | biological_process | phosphatidylinositol dephosphorylation |
D | 0016791 | molecular_function | phosphatase activity |
D | 0046856 | biological_process | phosphatidylinositol dephosphorylation |
E | 0016791 | molecular_function | phosphatase activity |
E | 0046856 | biological_process | phosphatidylinositol dephosphorylation |
F | 0016791 | molecular_function | phosphatase activity |
F | 0046856 | biological_process | phosphatidylinositol dephosphorylation |
G | 0016791 | molecular_function | phosphatase activity |
G | 0046856 | biological_process | phosphatidylinositol dephosphorylation |
H | 0016791 | molecular_function | phosphatase activity |
H | 0046856 | biological_process | phosphatidylinositol dephosphorylation |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 8 |
Details | binding site for residue B3P A 901 |
Chain | Residue |
A | GLY450 |
A | LEU451 |
A | THR454 |
A | ASP456 |
A | GLU457 |
A | ASP711 |
A | HOH1004 |
D | GLU642 |
site_id | AC2 |
Number of Residues | 3 |
Details | binding site for residue EDO A 902 |
Chain | Residue |
A | SER624 |
A | HOH1005 |
A | ILE623 |
site_id | AC3 |
Number of Residues | 6 |
Details | binding site for residue B3P B 901 |
Chain | Residue |
B | GLY450 |
B | GLY452 |
B | THR454 |
B | ASP456 |
B | GLU457 |
B | ASP711 |
site_id | AC4 |
Number of Residues | 7 |
Details | binding site for residue EDO B 902 |
Chain | Residue |
B | THR532 |
B | ILE534 |
B | GLN574 |
B | ASN575 |
B | ASP578 |
B | HOH1034 |
H | SER788 |
site_id | AC5 |
Number of Residues | 10 |
Details | binding site for residue EDO B 903 |
Chain | Residue |
B | THR759 |
B | ALA760 |
B | SER761 |
B | ARG762 |
B | ASN790 |
B | ILE791 |
B | PHE793 |
B | LEU794 |
H | GLN574 |
H | ASP578 |
site_id | AC6 |
Number of Residues | 4 |
Details | binding site for residue EDO B 904 |
Chain | Residue |
B | LEU455 |
B | THR461 |
B | ILE462 |
B | HIS464 |
site_id | AC7 |
Number of Residues | 9 |
Details | binding site for residue EDO B 905 |
Chain | Residue |
B | GLN574 |
B | ASP578 |
H | THR759 |
H | ALA760 |
H | SER788 |
H | ASN790 |
H | ILE791 |
H | PHE793 |
H | LEU794 |
site_id | AC8 |
Number of Residues | 4 |
Details | binding site for residue EDO B 906 |
Chain | Residue |
B | ALA755 |
B | LYS795 |
B | GLN797 |
E | GLN617 |
site_id | AC9 |
Number of Residues | 7 |
Details | binding site for residue PO4 C 901 |
Chain | Residue |
C | ASN432 |
C | HIS561 |
C | ASN609 |
C | HIS718 |
C | MG902 |
C | HOH1001 |
C | HOH1005 |
site_id | AD1 |
Number of Residues | 2 |
Details | binding site for residue MG C 902 |
Chain | Residue |
C | PO4901 |
C | HOH1005 |
site_id | AD2 |
Number of Residues | 8 |
Details | binding site for residue B3P C 903 |
Chain | Residue |
C | GLY450 |
C | LEU451 |
C | GLY452 |
C | LYS453 |
C | THR454 |
C | ASP456 |
C | GLU457 |
C | ASP711 |
site_id | AD3 |
Number of Residues | 10 |
Details | binding site for residue PO4 D 901 |
Chain | Residue |
D | ASN432 |
D | GLU473 |
D | HIS561 |
D | SER564 |
D | ASN609 |
D | TYR661 |
D | HIS718 |
D | MG902 |
D | HOH1002 |
D | HOH1021 |
site_id | AD4 |
Number of Residues | 4 |
Details | binding site for residue MG D 902 |
Chain | Residue |
D | GLU473 |
D | PO4901 |
D | HOH1002 |
D | HOH1021 |
site_id | AD5 |
Number of Residues | 6 |
Details | binding site for residue B3P D 903 |
Chain | Residue |
D | GLY450 |
D | GLY452 |
D | THR454 |
D | ASP456 |
D | GLU457 |
D | ASP711 |
site_id | AD6 |
Number of Residues | 10 |
Details | binding site for residue EDO D 904 |
Chain | Residue |
D | THR759 |
D | ALA760 |
D | SER761 |
D | ARG762 |
D | ASN790 |
D | ILE791 |
D | PHE793 |
D | LEU794 |
F | GLN574 |
F | ASP578 |
site_id | AD7 |
Number of Residues | 4 |
Details | binding site for residue EDO D 905 |
Chain | Residue |
D | SER547 |
D | GLY586 |
D | ASP587 |
D | HIS524 |
site_id | AD8 |
Number of Residues | 6 |
Details | binding site for residue EDO D 906 |
Chain | Residue |
D | THR532 |
D | GLY533 |
D | GLN574 |
D | ASN575 |
D | ASP578 |
F | SER788 |
site_id | AD9 |
Number of Residues | 9 |
Details | binding site for residue PO4 E 901 |
Chain | Residue |
E | ASN432 |
E | GLU473 |
E | HIS561 |
E | SER564 |
E | ASN609 |
E | TYR661 |
E | HIS718 |
E | MG902 |
E | HOH1004 |
site_id | AE1 |
Number of Residues | 4 |
Details | binding site for residue MG E 902 |
Chain | Residue |
E | ASN432 |
E | GLU473 |
E | PO4901 |
E | HOH1028 |
site_id | AE2 |
Number of Residues | 6 |
Details | binding site for residue B3P E 903 |
Chain | Residue |
E | GLY450 |
E | GLY452 |
E | THR454 |
E | ASP456 |
E | GLU457 |
E | ASP711 |
site_id | AE3 |
Number of Residues | 5 |
Details | binding site for residue EDO E 904 |
Chain | Residue |
E | PRO438 |
E | VAL442 |
E | TRP481 |
E | LEU484 |
E | HOH1002 |
site_id | AE4 |
Number of Residues | 5 |
Details | binding site for residue EDO E 905 |
Chain | Residue |
E | LEU455 |
E | VAL458 |
E | ILE462 |
E | HIS464 |
E | HOH1001 |
site_id | AE5 |
Number of Residues | 10 |
Details | binding site for residue PO4 F 901 |
Chain | Residue |
F | ASN432 |
F | GLU473 |
F | HIS561 |
F | SER564 |
F | ASN609 |
F | TYR661 |
F | HIS718 |
F | MG902 |
F | HOH1021 |
F | HOH1023 |
site_id | AE6 |
Number of Residues | 3 |
Details | binding site for residue MG F 902 |
Chain | Residue |
F | GLU473 |
F | PO4901 |
F | HOH1021 |
site_id | AE7 |
Number of Residues | 6 |
Details | binding site for residue B3P F 903 |
Chain | Residue |
F | GLY450 |
F | GLY452 |
F | THR454 |
F | ASP456 |
F | GLU457 |
F | ASP711 |
site_id | AE8 |
Number of Residues | 5 |
Details | binding site for residue EDO F 904 |
Chain | Residue |
F | HIS524 |
F | SER547 |
F | PHE548 |
F | GLY586 |
F | ASP587 |
site_id | AE9 |
Number of Residues | 5 |
Details | binding site for residue EDO F 905 |
Chain | Residue |
F | ALA592 |
F | ASP594 |
F | GLU836 |
F | HIS858 |
F | ARG859 |
site_id | AF1 |
Number of Residues | 4 |
Details | binding site for residue EDO F 906 |
Chain | Residue |
F | LEU455 |
F | VAL458 |
F | ILE462 |
F | HIS464 |
site_id | AF2 |
Number of Residues | 8 |
Details | binding site for residue EDO F 907 |
Chain | Residue |
D | GLN574 |
F | THR759 |
F | ALA760 |
F | SER788 |
F | ASN790 |
F | ILE791 |
F | PHE793 |
F | LEU794 |
site_id | AF3 |
Number of Residues | 6 |
Details | binding site for residue PO4 G 901 |
Chain | Residue |
G | HIS561 |
G | SER564 |
G | ASN609 |
G | HIS718 |
G | MG902 |
G | HOH1001 |
site_id | AF4 |
Number of Residues | 2 |
Details | binding site for residue MG G 902 |
Chain | Residue |
G | PO4901 |
G | HOH1007 |
site_id | AF5 |
Number of Residues | 4 |
Details | binding site for residue EDO G 903 |
Chain | Residue |
G | TYR622 |
G | GLU627 |
H | ASN792 |
H | PHE793 |
site_id | AF6 |
Number of Residues | 9 |
Details | binding site for residue PO4 H 901 |
Chain | Residue |
H | ASN432 |
H | GLU473 |
H | HIS561 |
H | SER564 |
H | ASN609 |
H | TYR661 |
H | HIS718 |
H | MG902 |
H | HOH1024 |
site_id | AF7 |
Number of Residues | 4 |
Details | binding site for residue MG H 902 |
Chain | Residue |
H | GLU473 |
H | PO4901 |
H | HOH1006 |
H | HOH1024 |
site_id | AF8 |
Number of Residues | 7 |
Details | binding site for residue B3P H 903 |
Chain | Residue |
H | GLY450 |
H | GLY452 |
H | THR454 |
H | ASP456 |
H | GLU457 |
H | ASP711 |
H | HOH1003 |
site_id | AF9 |
Number of Residues | 3 |
Details | binding site for residue EDO H 904 |
Chain | Residue |
H | SER771 |
H | THR772 |
H | HIS820 |