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 |
