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enzyme (lysozyme)

 
Enzymes
  Enzyme classes:
  EC 1: Oxidoreductases
  EC 2: Transferases
    EC 2.1
    EC 2.2
    EC 2.3
    EC 2.4
    EC 2.5
    EC 2.6
    EC 2.7
      EC 2.7.1
        EC 2.7.1.1
        EC 2.7.1.2
        EC 2.7.1.3
        EC 2.7.1.4
        EC 2.7.1.5
        EC 2.7.1.6
        EC 2.7.1.7
        EC 2.7.1.8
        EC 2.7.1.9
        EC 2.7.1.10
        EC 2.7.1.11
        EC 2.7.1.12
        EC 2.7.1.13
        EC 2.7.1.14
        EC 2.7.1.15
        EC 2.7.1.16
        EC 2.7.1.17
        EC 2.7.1.18
        EC 2.7.1.19
        EC 2.7.1.20
        EC 2.7.1.21
        EC 2.7.1.22
        EC 2.7.1.23
        EC 2.7.1.24
        EC 2.7.1.25
        EC 2.7.1.26
        EC 2.7.1.27
        EC 2.7.1.28
        EC 2.7.1.29
        EC 2.7.1.30
        EC 2.7.1.31
        EC 2.7.1.32
        EC 2.7.1.33
        EC 2.7.1.34
        EC 2.7.1.35
        EC 2.7.1.36
        EC 2.7.1.37
        EC 2.7.1.38
        EC 2.7.1.39
        EC 2.7.1.40
        EC 2.7.1.41
        EC 2.7.1.42
        EC 2.7.1.43
        EC 2.7.1.44
        EC 2.7.1.45
        EC 2.7.1.46
        EC 2.7.1.47
        EC 2.7.1.48
        EC 2.7.1.49
        EC 2.7.1.50
        EC 2.7.1.51
        EC 2.7.1.52
        EC 2.7.1.53
        EC 2.7.1.54
        EC 2.7.1.55
        EC 2.7.1.56
        EC 2.7.1.57
        EC 2.7.1.58
        EC 2.7.1.59
        EC 2.7.1.60
        EC 2.7.1.61
        EC 2.7.1.62
        EC 2.7.1.63
        EC 2.7.1.64
        EC 2.7.1.65
        EC 2.7.1.66
        EC 2.7.1.67
        EC 2.7.1.68
        EC 2.7.1.69
        EC 2.7.1.70
        EC 2.7.1.71
        EC 2.7.1.72
        EC 2.7.1.73
        EC 2.7.1.74
        EC 2.7.1.75
        EC 2.7.1.76
        EC 2.7.1.77
        EC 2.7.1.78
        EC 2.7.1.79
        EC 2.7.1.80
        EC 2.7.1.81
        EC 2.7.1.82
        EC 2.7.1.83
        EC 2.7.1.84
        EC 2.7.1.85
        EC 2.7.1.86
        EC 2.7.1.87
        EC 2.7.1.88
        EC 2.7.1.89
        EC 2.7.1.90
        EC 2.7.1.91
        EC 2.7.1.92
        EC 2.7.1.93
        EC 2.7.1.94
        EC 2.7.1.95
        EC 2.7.1.96
        EC 2.7.1.97
        EC 2.7.1.98
        EC 2.7.1.99
        EC 2.7.1.100
        EC 2.7.1.101
        EC 2.7.1.102
        EC 2.7.1.103
        EC 2.7.1.104
        EC 2.7.1.105
        EC 2.7.1.106
        EC 2.7.1.107
        EC 2.7.1.108
        EC 2.7.1.109
        EC 2.7.1.110
        EC 2.7.1.111
        EC 2.7.1.112
        EC 2.7.1.113
        EC 2.7.1.114
        EC 2.7.1.115
        EC 2.7.1.116
        EC 2.7.1.117
        EC 2.7.1.118
        EC 2.7.1.119
        EC 2.7.1.120
        EC 2.7.1.121
        EC 2.7.1.122
        EC 2.7.1.123
        EC 2.7.1.124
        EC 2.7.1.125
        EC 2.7.1.126
        EC 2.7.1.127
        EC 2.7.1.128
        EC 2.7.1.129
        EC 2.7.1.130
        EC 2.7.1.131
        EC 2.7.1.132
        EC 2.7.1.133
        EC 2.7.1.134
        EC 2.7.1.135
        EC 2.7.1.136
        EC 2.7.1.137
        EC 2.7.1.138
        EC 2.7.1.139
        EC 2.7.1.140
        EC 2.7.1.141
        EC 2.7.1.142
        EC 2.7.1.143
        EC 2.7.1.144
        EC 2.7.1.145
        EC 2.7.1.146
        EC 2.7.1.147
        EC 2.7.1.148
        EC 2.7.1.149
        EC 2.7.1.150
        EC 2.7.1.151
        EC 2.7.1.152
        EC 2.7.1.153
        EC 2.7.1.154
        EC 2.7.1.155
        EC 2.7.1.156
        EC 2.7.1.157
        EC 2.7.1.158
        EC 2.7.1.159
        EC 2.7.1.160
        EC 2.7.1.161
        EC 2.7.1.162
      EC 2.7.2
      EC 2.7.3
      EC 2.7.4
      EC 2.7.5
      EC 2.7.6
      EC 2.7.7
      EC 2.7.8
      EC 2.7.9
      EC 2.7.10
      EC 2.7.11
      EC 2.7.12
      EC 2.7.13
      EC 2.7.14
    EC 2.8
    EC 2.9
  EC 3: Hydrolases
  EC 4: Lyases
  EC 5: Isomerases
  EC 6: Ligases
  General information:
  Catalytic mechanism
  Enzyme kinetics
  Inhibitors
  Enzymes in industry

EC 2.7.1.137 - ATP:1- phosphatidyl- 1D- myo- inositol 3- phosphotransferase (phosphatidylinositol 3- kinase)



3D structures of EC 2.7.1.137 - phosphatidylinositol 3-kinase in Protein Data Bank

updated: 29 May 2015, 1:12

In total: 37 PDB structures of EC 2.7.1.137 - phosphatidylinositol 3-kinase:
  1. 1e7u: Structure Determinants of Phosphoinositide 3-kinase Inhibition by Wortmannin, Ly294002, Quercetin, Myricetin and Staurosporine
  2. 1e7v: Structure Determinants of Phosphoinositide 3-kinase Inhibition by Wortmannin, Ly294002, Quercetin, Myricetin and Staurosporine
  3. 1e8w: Structure Determinants of Phosphoinositide 3-kinase Inhibition by Wortmannin, Ly294002, Quercetin, Myricetin and Staurosporine
  4. 1e8x: Structural Insights into Phoshoinositide 3-kinase Enzymatic Mechanism and Signalling
  5. 1e8y: Structure Determinants of Phosphoinositide 3-kinase Inhibition by Wortmannin, Ly294002, Quercetin, Myricetin and Staurosporine
  6. 1e8z: Structure Determinants of Phosphoinositide 3-kinase Inhibition by Wortmannin, Ly294002, Quercetin, Myricetin and Staurosporine
  7. 1e90: Structure Determinants of Phosphoinositide 3-kinase Inhibition by Wortmannin, Ly294002, Quercetin, Myricetin and Staurosporine
  8. 1he8: Ras G12V - Pi 3-kinase Gamma Complex
  9. 3ls8: Crystal Structure of Human PIK3C3 in Complex with 3-[4-(4- Morpholinyl)thieno[3,2-d]pyrimidin-2-yl]-phenol
  10. 1pic: Phosphatidylinositol 3-kinase, P85-alpha Subunit: C- Terminal Sh2 Domain Complexed with a Tyr751 Phosphopeptide from The Pdgf Receptor, Nmr, Minimized Mean Structure
  11. 1pks: Structure of The PI3K Sh3 Domain and Analysis of The Sh3 Family
  12. 1pkt: Structure of The PI3K Sh3 Domain and Analysis of The Sh3 Family
  13. 3ihy: Human PIK3C3 Crystal Structure
  14. 1w1n: The Solution Structure of The Fatc Domain of The Protein Kinase Tor1 from Yeast
  15. 2x6k: The Crystal Structure of The Drosophila Class III Pi3-kinase Vps34 in Complex with Pi-103
  16. 2x6j: The Crystal Structure of The Drosophila Class III Pi3-kinase Vps34 in Complex with Pik-93
  17. 2x6i: The Crystal Structure of The Drosophila Class III Pi3-kinase Vps34 in Complex with Pik-90
  18. 2x6h: The Crystal Structure of The Drosophila Class III Pi3-kinase Vps34
  19. 2x6f: The Crystal Structure of The Drosophila Class III Pi3-kinase Vps34 in Complex with 3-methyladenine
  20. 2chw: A Pharmacological Map of The Pi3-k Family Defines a Role for P110 Alpha in Signaling: The Structure of Complex of Phosphoinositide 3-kinase Gamma with Inhibitor Pik-39
  21. 2chx: A Pharmacological Map of The Pi3-k Family Defines a Role for P110ALPHA in Signaling: The Structure of Complex of Phosphoinositide 3-kinase Gamma with Inhibitor Pik-90
  22. 2chz: A Pharmacological Map of The Pi3-k Family Defines a Role for P110ALPHA in Signaling: The Structure of Complex of Phosphoinositide 3-kinase Gamma with Inhibitor Pik-93
  23. 2pnb: Structure of an Sh2 Domain of The P85 Alpha Subunit of Phosphatidylinositol-3-oh Kinase
  24. 2pna: Structure of an Sh2 Domain of The P85 Alpha Subunit of Phosphatidylinositol-3-oh Kinase
  25. 2iwl: Structure of The Px Domain of Phosphoinositide 3-kinase- C2ALPHA
  26. 3zvv: Fragment Bound to PI3KINASE Gamma
  27. 4anu: Complexes of PI3KGAMMA with Isoform Selective Inhibitors.
  28. 4anv: Complexes of PI3KGAMMA with Isoform Selective Inhibitors.
  29. 4anw: Complexes of PI3KGAMMA with Isoform Selective Inhibitors.
  30. 4anx: Complexes of PI3KGAMMA with Isoform Selective Inhibitors.
  31. 4oys: Crystal Structure of Vps34 in Complex with Sar405.
  32. 4ph4: The Crystal Structure of Human Vps34 in Complex with Pik-iii
  33. 4uwf: Discovery of (2s)-8-((3r)-3-methylmorpholin-4-yl)-1-(3- Methyl-2-oxo-butyl)-2-(trifluoromethyl)-3,4-dihydro-2h- Pyrimido(1,2-a)pyrimidin-6-one: a Novel Potent and Selective Inhibitor of Vps34 for The Treatment of Solid Tumors
  34. 4uwg: Discovery of (2s)-8-((3r)-3-methylmorpholin-4-yl)-1-(3- Methyl-2-oxo-butyl)-2-(trifluoromethyl)-3,4-dihydro-2h- Pyrimido(1,2-a)pyrimidin-6-one: a Novel Potent and Selective Inhibitor of Vps34 for The Treatment of Solid Tumors
  35. 4uwh: Discovery of (2s)-8-((3r)-3-methylmorpholin-4-yl)-1-(3- Methyl-2-oxo-butyl)-2-(trifluoromethyl)-3,4-dihydro-2h- Pyrimido(1,2-a)pyrimidin-6-one: a Novel Potent and Selective Inhibitor of Vps34 for The Treatment of Solid Tumors
  36. 4uwk: Discovery of (2s)-8-((3r)-3-methylmorpholin-4-yl)-1-(3- Methyl-2-oxo-butyl)-2-(trifluoromethyl)-3,4-dihydro-2h- Pyrimido(1,2-a)pyrimidin-6-one: a Novel Potent and Selective Inhibitor of Vps34 for The Treatment of Solid Tumors
  37. 4uwl: Discovery of (2s)-8-((3r)-3-methylmorpholin-4-yl)-1-(3- Methyl-2-oxo-butyl)-2-(trifluoromethyl)-3,4-dihydro-2h- Pyrimido(1,2-a)pyrimidin-6-one: a Novel Potent and Selective Inhibitor of Vps34 for The Treatment of Solid Tumors
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