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enzyme (lysozyme)

 
Enzymes
  Enzyme classes:
  EC 1: Oxidoreductases
  EC 2: Transferases
  EC 3: Hydrolases
    EC 3.1
    EC 3.2
    EC 3.3
    EC 3.4
      EC 3.4.1
      EC 3.4.2
      EC 3.4.3
      EC 3.4.4
      EC 3.4.11
      EC 3.4.12
      EC 3.4.13
      EC 3.4.14
      EC 3.4.15
      EC 3.4.16
      EC 3.4.17
      EC 3.4.18
      EC 3.4.19
      EC 3.4.21
      EC 3.4.22
        EC 3.4.22.1
        EC 3.4.22.2
        EC 3.4.22.3
        EC 3.4.22.4
        EC 3.4.22.5
        EC 3.4.22.6
        EC 3.4.22.7
        EC 3.4.22.8
        EC 3.4.22.9
        EC 3.4.22.10
        EC 3.4.22.11
        EC 3.4.22.12
        EC 3.4.22.13
        EC 3.4.22.14
        EC 3.4.22.15
        EC 3.4.22.16
        EC 3.4.22.17
        EC 3.4.22.18
        EC 3.4.22.19
        EC 3.4.22.20
        EC 3.4.22.21
        EC 3.4.22.22
        EC 3.4.22.23
        EC 3.4.22.24
        EC 3.4.22.25
        EC 3.4.22.26
        EC 3.4.22.27
        EC 3.4.22.28
        EC 3.4.22.29
        EC 3.4.22.30
        EC 3.4.22.31
        EC 3.4.22.32
        EC 3.4.22.33
        EC 3.4.22.34
        EC 3.4.22.35
        EC 3.4.22.36
        EC 3.4.22.37
        EC 3.4.22.38
        EC 3.4.22.39
        EC 3.4.22.40
        EC 3.4.22.41
        EC 3.4.22.42
        EC 3.4.22.43
        EC 3.4.22.44
        EC 3.4.22.45
        EC 3.4.22.46
        EC 3.4.22.47
        EC 3.4.22.48
        EC 3.4.22.49
        EC 3.4.22.50
        EC 3.4.22.51
        EC 3.4.22.52
        EC 3.4.22.53
        EC 3.4.22.54
        EC 3.4.22.55
        EC 3.4.22.56
        EC 3.4.22.57
        EC 3.4.22.58
        EC 3.4.22.59
        EC 3.4.22.60
        EC 3.4.22.61
        EC 3.4.22.62
        EC 3.4.22.63
        EC 3.4.22.64
        EC 3.4.22.65
        EC 3.4.22.66
        EC 3.4.22.67
        EC 3.4.22.68
      EC 3.4.23
      EC 3.4.24
      EC 3.4.25
      EC 3.4.99
    EC 3.5
    EC 3.6
    EC 3.7
    EC 3.8
    EC 3.9
    EC 3.10
    EC 3.11
    EC 3.12
    EC 3.13
  EC 4: Lyases
  EC 5: Isomerases
  EC 6: Ligases
  General information:
  Catalytic mechanism
  Enzyme kinetics
  Inhibitors
  Enzymes in industry

EC 3.4.22.15 - cathepsin L



3D structures of EC 3.4.22.15 - cathepsin L in Protein Data Bank

updated: 6 January 2022, 2:15

In total: 46 PDB structures of EC 3.4.22.15 - cathepsin L:
  1. 1cjl: Crystal Structure of a Cysteine Protease Proform
  2. 1cs8: Crystal Structure of Procathepsin L
  3. 1icf: Crystal Structure of Mhc Class II Associated P41 II Fragment in Complex with Cathepsin L
  4. 1mhw: Design of Non-covalent Inhibitors of Human Cathepsin L. from The 96-residue Proregion to Optimized Tripeptides
  5. 3kse: Unreduced Cathepsin L in Complex with Stefin a
  6. 3k24: Crystal Structure of Mature Apo-cathepsin L C25A Mutant in Complex with Gln-leu-ala Peptide
  7. 3iv2: Crystal Structure of Mature Apo-cathepsin L C25A Mutant
  8. 3hwn: Cathepsin L with Az13010160
  9. 3hha: Crystal Structure of Cathepsin L in Complex with Az12878478
  10. 3h8c: A Combined Crystallographic and Molecular Dynamics Study of Cathepsin-l Retro-binding Inhibitors (compound 14)
  11. 3h8b: A Combined Crystallographic and Molecular Dynamics Study of Cathepsin-l Retro-binding Inhibitors(compound 9)
  12. 3h89: A Combined Crystallographic and Molecular Dynamics Study of Cathepsin-l Retro-binding Inhibitors(compound 4)
  13. 3f75: Activated Toxoplasma Gondii Cathepsin L (tgcpl) in Complex with Its Propeptide
  14. 3bc3: Exploring Inhibitor Binding at The S Subsites of Cathepsin L
  15. 7avm: Crystal Structure of Pro-rhodesain C150A
  16. 6jd8: Structure of a Proline Specific Mutant of Human Cathepsin L
  17. 2p86: The High Resolution Crystal Structure of Rohedsain, The Major Cathepsin L Protease from T. Brucei Rhodesiense, Bound to Inhibitor K11002
  18. 2o6x: Crystal Structure of Procathepsin L1 from Fasciola Hepatica
  19. 2nqd: Crystal Structure of Cysteine Protease Inhibitor, Chagasin, in Complex with Human Cathepsin L
  20. 3of8: Structural Basis for Reversible and Irreversible Inhibition of Human Cathepsin L by Their Respective Dipeptidyl Glyoxal and Diazomethylketone Inhibitors
  21. 3of9: Structural Basis for Irreversible Inhibition of Human Cathepsin L by a Diazomethylketone Inhibitor
  22. 2xu1: Cathepsin L with a Nitrile Inhibitor
  23. 2xu3: Cathepsin L with a Nitrile Inhibitor
  24. 2xu4: Cathepsin L with a Nitrile Inhibitor
  25. 2xu5: Cathepsin L with a Nitrile Inhibitor
  26. 6jd0: Structure of Mutant Human Cathepsin L, Engineered for Gag Binding
  27. 2yj2: Cathepsin L with a Nitrile Inhibitor
  28. 2yj8: Cathepsin L with a Nitrile Inhibitor
  29. 2yj9: Cathepsin L with a Nitrile Inhibitor
  30. 2yjb: Cathepsin L with a Nitrile Inhibitor
  31. 2yjc: Cathepsin L with a Nitrile Inhibitor
  32. 3qj3: Structure of Digestive Procathepsin L2 Proteinase from Tenebrio Molitor Larval Midgut
  33. 3qt4: Structure of Digestive Procathepsin L 3 of Tenebrio Molitor Larval Midgut
  34. 4axl: Human Cathepsin L Apo Form with Zn
  35. 4axm: Triazine Cathepsin Inhibitor Complex
  36. 6f06: Cathepsin L in Complex with (3s,14e)-8-(azetidin-3-yl)-19-chloro-n-(1- Cyanocyclopropyl)-5-oxo-12,17-dioxa-4-azatricyclo[16.2.2.06, 11]docosa-1(21),6,8,10,14,18(22),19-heptaene-3-carboxamide
  37. 6ezx: Cathepsin L in Complex with (3s,14e)-19-chloro-n-(1-cyanocyclopropyl)- 5-oxo-17-oxa-4-azatricyclo[16.2.2.06,11]docosa-1(21),6,8,10,14, 18(22),19-heptaene-3-carboxamide
  38. 6ezp: Cathepsin L in Complex with (3s,14e)-19-chloro-n-(1-cyanocyclopropyl)- 5-oxo-12,17-dioxa-4-azatricyclo[16.2.2.06,11]docosa-1(21),6(11),7,9, 14,18(22),19-heptaene-3-carboxamide
  39. 4ci7: The Crystal Structure of The Cysteine Protease and Lectin-like Domains of Cwp84, a Surface Layer Associated Protein of Clostridium Difficile
  40. 5mqy: Cathepsin L in Complex with 4-[1,3-benzodioxol-5-ylmethyl(2- Phenoxyethyl)amino]-5-fluoropyrimidine-2-carbonitrile
  41. 5maj: Cathepsin L in Complex with 4-[cyclopentyl(imidazo[1,2-a]pyridin-2- Ylmethyl)amino]-6-morpholino-1,3,5-triazine-2-carbonitrile
  42. 5mae: Cathepsin L in Complex with (2s,4r)-4-(2-chloro-4-methoxy- Benzenesulfonyl)-1-[3-(5-chloro-pyridin-2-yl)-azetidine-3-carbonyl]- Pyrrolidine-2-car Boxylic Acid (1-cyano-cyclopropyl)-amide
  43. 5i4h: Caught in The Act: The Crystal Structure of Cleaved Cathepsin L Bound to The Active Site of Cathepsin L
  44. 5f02: Cathepsin L in Complex with (2s,4r)-4-(2-chloro-4-methoxy- Benzenesulfonyl)-1-[3-(5-chloro-pyridin-2-yl)-azetidine-3-carbonyl]- Pyrrolidine-2-carboxylic Acid (1-cyano-cyclopropyl)-amide
  45. 4d59: Clostridial Cysteine Protease Cwp84 C116A after Propeptide Cleavage
  46. 4d5a: Clostridial Cysteine Protease Cwp84 C116A after Propeptide Cleavage
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