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enzyme (lysozyme)

 
Enzymes
  Enzyme classes:
  EC 1: Oxidoreductases
    EC 1.1
    EC 1.2
    EC 1.3
    EC 1.4
    EC 1.5
    EC 1.6
    EC 1.7
    EC 1.8
    EC 1.9
    EC 1.10
    EC 1.11
    EC 1.12
    EC 1.13
    EC 1.14
      EC 1.14.1
      EC 1.14.2
      EC 1.14.3
      EC 1.14.11
      EC 1.14.12
      EC 1.14.13
        EC 1.14.13.1
        EC 1.14.13.2
        EC 1.14.13.3
        EC 1.14.13.4
        EC 1.14.13.5
        EC 1.14.13.6
        EC 1.14.13.7
        EC 1.14.13.8
        EC 1.14.13.9
        EC 1.14.13.10
        EC 1.14.13.11
        EC 1.14.13.12
        EC 1.14.13.13
        EC 1.14.13.14
        EC 1.14.13.15
        EC 1.14.13.16
        EC 1.14.13.17
        EC 1.14.13.18
        EC 1.14.13.19
        EC 1.14.13.20
        EC 1.14.13.21
        EC 1.14.13.22
        EC 1.14.13.23
        EC 1.14.13.24
        EC 1.14.13.25
        EC 1.14.13.26
        EC 1.14.13.27
        EC 1.14.13.28
        EC 1.14.13.29
        EC 1.14.13.30
        EC 1.14.13.31
        EC 1.14.13.32
        EC 1.14.13.33
        EC 1.14.13.34
        EC 1.14.13.35
        EC 1.14.13.36
        EC 1.14.13.37
        EC 1.14.13.38
        EC 1.14.13.39
        EC 1.14.13.40
        EC 1.14.13.41
        EC 1.14.13.42
        EC 1.14.13.43
        EC 1.14.13.44
        EC 1.14.13.45
        EC 1.14.13.46
        EC 1.14.13.47
        EC 1.14.13.48
        EC 1.14.13.49
        EC 1.14.13.50
        EC 1.14.13.51
        EC 1.14.13.52
        EC 1.14.13.53
        EC 1.14.13.54
        EC 1.14.13.55
        EC 1.14.13.56
        EC 1.14.13.57
        EC 1.14.13.58
        EC 1.14.13.59
        EC 1.14.13.60
        EC 1.14.13.61
        EC 1.14.13.62
        EC 1.14.13.63
        EC 1.14.13.64
        EC 1.14.13.65
        EC 1.14.13.66
        EC 1.14.13.67
        EC 1.14.13.68
        EC 1.14.13.69
        EC 1.14.13.70
        EC 1.14.13.71
        EC 1.14.13.72
        EC 1.14.13.73
        EC 1.14.13.74
        EC 1.14.13.75
        EC 1.14.13.76
        EC 1.14.13.77
        EC 1.14.13.78
        EC 1.14.13.79
        EC 1.14.13.80
        EC 1.14.13.81
        EC 1.14.13.82
        EC 1.14.13.83
        EC 1.14.13.84
        EC 1.14.13.85
        EC 1.14.13.86
        EC 1.14.13.87
        EC 1.14.13.88
        EC 1.14.13.89
        EC 1.14.13.90
        EC 1.14.13.91
        EC 1.14.13.92
        EC 1.14.13.93
        EC 1.14.13.94
        EC 1.14.13.95
        EC 1.14.13.96
        EC 1.14.13.97
        EC 1.14.13.98
        EC 1.14.13.99
        EC 1.14.13.100
        EC 1.14.13.101
        EC 1.14.13.102
        EC 1.14.13.103
        EC 1.14.13.104
        EC 1.14.13.105
      EC 1.14.14
      EC 1.14.15
      EC 1.14.16
      EC 1.14.17
      EC 1.14.18
      EC 1.14.19
      EC 1.14.20
      EC 1.14.21
      EC 1.14.99
    EC 1.15
    EC 1.16
    EC 1.17
    EC 1.18
    EC 1.19
    EC 1.20
    EC 1.21
    EC 1.97
    EC 1.98
    EC 1.99
  EC 2: Transferases
  EC 3: Hydrolases
  EC 4: Lyases
  EC 5: Isomerases
  EC 6: Ligases
  General information:
  Catalytic mechanism
  Enzyme kinetics
  Inhibitors
  Enzymes in industry

EC 1.14.13.2 - 4- hydroxybenzoate,NADPH:oxygen oxidoreductase (3- hydroxylating) (4- hydroxybenzoate 3- monooxygenase)



3D structures of EC 1.14.13.2 - 4-hydroxybenzoate 3-monooxygenase in Protein Data Bank

updated: 6 January 2022, 2:15

In total: 33 PDB structures of EC 1.14.13.2 - 4-hydroxybenzoate 3-monooxygenase:
  1. 1bf3: P-hydroxybenzoate Hydroxylase (phbh) Mutant with Cys 116 Replaced by Ser (C116S) and Arg 42 Replaced by Lys (R42K), in Complex with Fad and 4-hydroxybenzoic Acid
  2. 1bgj: P-hydroxybenzoate Hydroxylase (phbh) Mutant with Cys 116 Replaced by Ser (C116S) and His 162 Replaced by Arg (H162R), in Complex with Fad and 4-hydroxybenzoic Acid
  3. 1bgn: P-hydroxybenzoate Hydroxylase (phbh) Mutant with Cys 116 Replaced by Ser (C116S) and Arg 269 Replaced by Thr (R269T), in Complex with Fad and 4-hydroxybenzoic Acid
  4. 1bkw: P-hydroxybenzoate Hydroxylase (phbh) Mutant with Cys116 Replaced by Ser (C116S) and Arg44 Replaced by Lys (R44K), in Complex with Fad and 4-hydroxybenzoic Acid
  5. 1cc4: Phe161 and Arg166 Variants of P-hydroxybenzoate Hydroxylase. Implications for Nadph Recognition and Structural Stability.
  6. 1cc6: Phe161 and Arg166 Variants of P-hydroxybenzoate Hydroxylase. Implications for Nadph Recognition and Structural Stability.
  7. 1cj2: Mutant GLN34ARG of Para-hydroxybenzoate Hydroxylase
  8. 1cj3: Mutant TYR38GLU of Para-hydroxybenzoate Hydroxylase
  9. 1cj4: Mutant Q34T of Para-hydroxybenzoate Hydroxylase
  10. 1d7l: Structure-function Correlations of The Reaction of Reduced Nicotinamide Analogs with P-hydroxybenzoate Hydroxylase Substituted with a Series of 8-substituted Flavins
  11. 1ius: P-hydroxybenzoate Hydroxylase Complexed with 4- Aminobenzoate at Ph 5.0
  12. 1iut: P-hydroxybenzoate Hydroxylase Complexed with 4- Aminobenzoate at Ph 7.4
  13. 1iuu: P-hydroxybenzoate Hydroxylase Complexed with 4- Aminobenzoate at Ph 9.4
  14. 1iuv: P-hydroxybenzoate Hydroxylase Complexed with 4-4- Hydroxybenzoate at Ph 5.0
  15. 1iuw: P-hydroxybenzoate Hydroxylase Complexed with 4-4- Hydroxybenzoate at Ph 7.4
  16. 1iux: P-hydroxybenzoate Hydroxylase Complexed with 4-4- Hydroxybenzoate at Ph 9.4
  17. 1k0i: Pseudomonas Aeruginosa Phbh R220Q in Complex with 100mm Phb
  18. 1k0j: Pseudomonas Aeruginosa Phbh R220Q in Complex with Nadph and Free of P-ohb
  19. 1k0l: Pseudomonas Aeruginosa Phbh R220Q Free of P-ohb
  20. 1pbb: Crystal Structures of Wild-type P-hydroxybenzoate Hydroxylase Complexed with 4-aminobenzoate, 2,4- Dihydroxybenzoate and 2-hydroxy-4-aminobenzoate and of The TRY222ALA Mutant, Complexed with 2-hydroxy-4- Aminobenzoate. Evidence for a Proton Channel and a New Binding Mode of The Flavin Ring
  21. 1pbc: Crystal Structures of Wild-type P-hydroxybenzoate Hydroxylase Complexed with 4-aminobenzoate, 2,4- Dihydroxybenzoate and 2-hydroxy-4-aminobenzoate and of The TRY222ALA Mutant, Complexed with 2-hydroxy-4- Aminobenzoate. Evidence for a Proton Channel and a New Binding Mode of The Flavin Ring
  22. 1pbd: Crystal Structures of Wild-type P-hydroxybenzoate Hydroxylase Complexed with 4-aminobenzoate, 2,4- Dihydroxybenzoate and 2-hydroxy-4-aminobenzoate and of The TRY222ALA Mutant, Complexed with 2-hydroxy-4- Aminobenzoate. Evidence for a Proton Channel and a New Binding Mode of The Flavin Ring
  23. 1pbe: Crystal Structure of The P-hydroxybenzoate Hydroxylase- Substrate Complex Refined at 1.9 Angstroms Resolution. Analysis of The Enzyme-substrate and Enzyme-product Complexes
  24. 1pbf: Crystal Structures of Wild-type P-hydroxybenzoate Hydroxylase Complexed with 4-aminobenzoate, 2,4- Dihydroxybenzoate and 2-hydroxy-4-aminobenzoate and of The TRY222ALA Mutant, Complexed with 2-hydroxy-4- Aminobenzoate. Evidence for a Proton Channel and a New Binding Mode of The Flavin Ring
  25. 1pdh: Crystal Structure of P-hydroxybenzoate Hydroxylase Reconstituted with The Modified Fad Present in Alcohol Oxidase from Methylotrophic Yeasts: Evidence for an Arabinoflavin
  26. 1phh: Crystal Structure of P-hydroxybenzoate Hydroxylase Complexed with Its Reaction Product 3,4-dihydroxybenzoate
  27. 1pxa: Crystal Structures of Mutant Pseudomonas Aeruginosa P- Hydroxybenzoate Hydroxylase: The TYR201PHE, TYR385PHE, and ASN300ASP Variants
  28. 1pxb: Crystal Structures of Mutant Pseudomonas Aeruginosa P- Hydroxybenzoate Hydroxylase: The TYR201PHE, TYR385PHE, and ASN300ASP Variants
  29. 1pxc: Crystal Structures of Mutant Pseudomonas Aeruginosa P- Hydroxybenzoate Hydroxylase: The TYR201PHE, TYR385PHE, and ASN300ASP Variants
  30. 1ykj: A45G P-hydroxybenzoate Hydroxylase with P-hydroxybenzoate Bound
  31. 2phh: The Coenzyme Analogue Adenosine 5-diphosphoribose Displaces Fad in The Active Site of P-hydroxybenzoate Hydroxylase. an X-ray Crystallographic Investigation
  32. 6ju1: P-hydroxybenzoate Hydroxylase Y385F Mutant Complexed with 3,4- Dihydroxybenzoate
  33. 6dll: 2.2 Angstrom Resolution Crystal Structure of P-hydroxybenzoate Hydroxylase from Pseudomonas Putida in Complex with Fad.
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