5OKM
Crystal structure of human SHIP2 Phosphatase-C2
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 | 9 |
Details | binding site for residue B3P A 901 |
Chain | Residue |
A | GLY450 |
A | GLY452 |
A | THR454 |
A | ASP456 |
A | GLU457 |
A | ASP711 |
A | HOH1006 |
A | HOH1018 |
A | HOH1159 |
site_id | AC2 |
Number of Residues | 8 |
Details | binding site for residue NO3 A 902 |
Chain | Residue |
A | GLY477 |
A | ASP478 |
A | ARG479 |
A | HOH1013 |
A | HOH1036 |
B | LEU505 |
B | TRP506 |
B | LYS531 |
site_id | AC3 |
Number of Residues | 4 |
Details | binding site for residue EDO A 903 |
Chain | Residue |
A | ALA592 |
A | HIS858 |
A | HOH1019 |
A | HOH1114 |
site_id | AC4 |
Number of Residues | 4 |
Details | binding site for residue EDO A 904 |
Chain | Residue |
A | SER624 |
A | ASP669 |
A | TYR671 |
A | HOH1104 |
site_id | AC5 |
Number of Residues | 5 |
Details | binding site for residue EDO A 905 |
Chain | Residue |
A | LEU455 |
A | THR461 |
A | ILE462 |
A | HIS464 |
A | HOH1064 |
site_id | AC6 |
Number of Residues | 4 |
Details | binding site for residue EDO A 906 |
Chain | Residue |
A | LYS626 |
A | GLU627 |
A | PHE628 |
A | GLU629 |
site_id | AC7 |
Number of Residues | 5 |
Details | binding site for residue EDO A 907 |
Chain | Residue |
A | HIS524 |
A | SER547 |
A | PHE548 |
A | GLY586 |
A | ASP587 |
site_id | AC8 |
Number of Residues | 10 |
Details | binding site for residue B3P B 901 |
Chain | Residue |
B | GLY450 |
B | GLY452 |
B | THR454 |
B | ASP456 |
B | GLU457 |
B | ASP711 |
B | HOH1017 |
B | HOH1024 |
B | HOH1071 |
B | HOH1114 |
site_id | AC9 |
Number of Residues | 7 |
Details | binding site for residue EDO B 902 |
Chain | Residue |
B | THR532 |
B | GLY533 |
B | GLN574 |
B | ASN575 |
B | ASP578 |
B | HOH1002 |
H | SER788 |
site_id | AD1 |
Number of Residues | 8 |
Details | binding site for residue EDO B 903 |
Chain | Residue |
B | THR759 |
B | ALA760 |
B | SER788 |
B | ASN790 |
B | PHE793 |
B | LEU794 |
B | HOH1025 |
H | GLN574 |
site_id | AD2 |
Number of Residues | 7 |
Details | binding site for residue EDO B 904 |
Chain | Residue |
B | LEU455 |
B | VAL458 |
B | THR461 |
B | ILE462 |
B | HIS464 |
B | HOH1038 |
B | HOH1043 |
site_id | AD3 |
Number of Residues | 5 |
Details | binding site for residue EDO B 905 |
Chain | Residue |
B | ALA755 |
B | LYS795 |
B | VAL796 |
B | GLN797 |
E | GLN617 |
site_id | AD4 |
Number of Residues | 10 |
Details | binding site for residue B3P C 901 |
Chain | Residue |
C | GLY450 |
C | GLY452 |
C | LYS453 |
C | THR454 |
C | ASP456 |
C | GLU457 |
C | ASP711 |
C | HOH1021 |
C | HOH1024 |
C | HOH1046 |
site_id | AD5 |
Number of Residues | 8 |
Details | binding site for residue NO3 C 902 |
Chain | Residue |
C | GLY477 |
C | ASP478 |
C | ARG479 |
C | HOH1005 |
C | HOH1020 |
H | LEU505 |
H | TRP506 |
H | LYS531 |
site_id | AD6 |
Number of Residues | 6 |
Details | binding site for residue EDO C 903 |
Chain | Residue |
C | HOH1081 |
C | ASN638 |
C | GLU652 |
C | GLU653 |
C | GLU654 |
C | ILE655 |
site_id | AD7 |
Number of Residues | 8 |
Details | binding site for residue B3P D 901 |
Chain | Residue |
D | GLY450 |
D | GLY452 |
D | THR454 |
D | ASP456 |
D | GLU457 |
D | ASP711 |
D | HOH1013 |
D | HOH1062 |
site_id | AD8 |
Number of Residues | 5 |
Details | binding site for residue EDO D 902 |
Chain | Residue |
D | HIS524 |
D | SER547 |
D | PHE548 |
D | GLY586 |
D | ASP587 |
site_id | AD9 |
Number of Residues | 5 |
Details | binding site for residue EDO D 903 |
Chain | Residue |
A | GLN797 |
A | HOH1003 |
D | TRP506 |
D | GLY539 |
D | ASN540 |
site_id | AE1 |
Number of Residues | 9 |
Details | binding site for residue EDO D 904 |
Chain | Residue |
D | THR759 |
D | ALA760 |
D | SER761 |
D | SER788 |
D | ASN790 |
D | PHE793 |
D | LEU794 |
F | GLN574 |
F | HOH1030 |
site_id | AE2 |
Number of Residues | 5 |
Details | binding site for residue EDO D 905 |
Chain | Residue |
D | THR532 |
D | GLY533 |
D | GLN574 |
D | ASN575 |
D | ASP578 |
site_id | AE3 |
Number of Residues | 6 |
Details | binding site for residue EDO D 906 |
Chain | Residue |
A | GLN617 |
D | GLU754 |
D | ALA755 |
D | LYS795 |
D | VAL796 |
D | GLN797 |
site_id | AE4 |
Number of Residues | 10 |
Details | binding site for residue B3P E 901 |
Chain | Residue |
B | GLU642 |
E | GLY450 |
E | GLY452 |
E | LYS453 |
E | THR454 |
E | ASP456 |
E | GLU457 |
E | ASP711 |
E | HOH1019 |
E | HOH1037 |
site_id | AE5 |
Number of Residues | 10 |
Details | binding site for residue B3P F 901 |
Chain | Residue |
F | GLY450 |
F | GLY452 |
F | THR454 |
F | ASP456 |
F | GLU457 |
F | ASP711 |
F | HOH1001 |
F | HOH1008 |
F | HOH1010 |
F | HOH1054 |
site_id | AE6 |
Number of Residues | 6 |
Details | binding site for residue EDO F 902 |
Chain | Residue |
F | ALA592 |
F | ASP594 |
F | GLU836 |
F | HIS858 |
F | ARG859 |
F | HOH1003 |
site_id | AE7 |
Number of Residues | 4 |
Details | binding site for residue EDO F 903 |
Chain | Residue |
F | VAL458 |
F | ILE462 |
F | HIS464 |
F | HOH1048 |
site_id | AE8 |
Number of Residues | 9 |
Details | binding site for residue EDO F 904 |
Chain | Residue |
D | GLN574 |
D | HOH1012 |
F | THR759 |
F | ALA760 |
F | SER788 |
F | ASN790 |
F | ILE791 |
F | PHE793 |
F | LEU794 |
site_id | AE9 |
Number of Residues | 6 |
Details | binding site for residue EDO F 905 |
Chain | Residue |
F | HIS524 |
F | SER547 |
F | PHE548 |
F | GLY586 |
F | ASP587 |
F | PHE599 |
site_id | AF1 |
Number of Residues | 3 |
Details | binding site for residue EDO G 901 |
Chain | Residue |
G | GLU627 |
G | HOH1003 |
H | PHE793 |
site_id | AF2 |
Number of Residues | 12 |
Details | binding site for residue B3P H 901 |
Chain | Residue |
H | GLY450 |
H | GLY452 |
H | LYS453 |
H | THR454 |
H | ASP456 |
H | GLU457 |
H | ASP711 |
H | HOH1003 |
H | HOH1025 |
H | HOH1078 |
H | HOH1081 |
H | HOH1085 |
site_id | AF3 |
Number of Residues | 8 |
Details | binding site for residue EDO H 902 |
Chain | Residue |
B | GLN574 |
H | THR759 |
H | ALA760 |
H | SER788 |
H | ASN790 |
H | PHE793 |
H | LEU794 |
H | HOH1044 |