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• 20:20, 30 April 2021 (hist) (diff) User:Alexandra Gredová‎ (top)
• 20:19, 30 April 2021 (hist) (diff) Image:Fig 4 4 4.jpg‎ (Fig. 4. Close-up to Arg158 residue interaction with Glu280 residue and Tyr268 residue. Hydrogen-bonds are shown here as red dashed lines (Erlandsen H, Stevens RC, 1999)) (top)
• 20:15, 30 April 2021 (hist) (diff) User:Alexandra Gredová‎
• 20:11, 30 April 2021 (hist) (diff) User:Alexandra Gredová‎
• 20:09, 30 April 2021 (hist) (diff) Image:Fig 5 5.png‎ (Fig. 5. Close-up to Arg261 residue interaction with Gln304 residue and Thr238 residue. Hydrogen-bonds are shown here as red dashed lines (Erlandsen H, Stevens RC, 1999)) (top)
• 20:07, 30 April 2021 (hist) (diff) Image:Fig 4 4.jpg‎ (Fig. 4. Close-up to Arg158 residue interaction with Glu280 residue and Tyr268 residue. Hydrogen-bonds are shown here as red dashed lines (Erlandsen H, Stevens RC, 1999)) (top)
• 20:04, 30 April 2021 (hist) (diff) Image:Fig 3 3.jpg‎ (Fig. 3. Close-up to Arg408 residue interaction with Leu308 residue and Leu311 residue. Hydrogen-bonds are shown here as red dashed lines (Erlandsen H, Stevens RC, 1999)) (top)
• 19:58, 30 April 2021 (hist) (diff) User:Alexandra Gredová‎
• 19:57, 30 April 2021 (hist) (diff) User:Alexandra Gredová‎
• 19:52, 30 April 2021 (hist) (diff) User:Alexandra Gredová‎
• 19:50, 30 April 2021 (hist) (diff) Image:Obraz5.png‎ (Fig. 5. Close-up to Arg261 residue interaction with Gln304 residue and Thr238 residue. Hydrogen-bonds are shown here as red dashed lines (Erlandsen H, Stevens RC, 1999)) (top)
• 19:49, 30 April 2021 (hist) (diff) Image:Obraz 5.png‎ (Fig. 5. Close-up to Arg261 residue interaction with Gln304 residue and Thr238 residue. Hydrogen-bonds are shown here as red dashed lines (Erlandsen H, Stevens RC, 1999)) (top)
• 19:47, 30 April 2021 (hist) (diff) Image:Obraz 4.png‎ (Fig. 4. Close-up to Arg158 residue interaction with Glu280 residue and Tyr268 residue. Hydrogen-bonds are shown here as red dashed lines (Erlandsen H, Stevens RC, 1999)) (top)
• 19:46, 30 April 2021 (hist) (diff) User:Alexandra Gredová‎
• 19:35, 30 April 2021 (hist) (diff) Image:Obraz 2.png‎ (Fig. 2. Model of domain organization in one PAH monomer. Regulatory N-terminal domain is in blue, catalytic C-terminal domain is in yellow, tetramerization domain is in green, iron ion bound by the catalytic domain is in red (Erlandsen H, Stevens RC, 1999) (top)
• 19:32, 30 April 2021 (hist) (diff) Image:Obraz 1.jpg‎ (Fig. 1. Crystal structure of human tetrameric PAH. Each monomere binds BH4 molecule as a cofactor which is shown here as spheres. The homo-tetrameric PAH has a two-fold symetry, which is drawn here as dashed black line (Flydal, M. I. et al., 2019)) (top)
• 19:21, 30 April 2021 (hist) (diff) Image:Obr.2.png‎ (Fig. 2. Model of domain organization in one PAH monomer. Regulatory N-terminal domain is in blue, catalytic C-terminal domain is in yellow, tetramerization domain is in green, iron ion bound by the catalytic domain is in red (12).) (top)
• 19:18, 30 April 2021 (hist) (diff) Image:Fig.1.png‎ (Crystal structure of human tetrameric PAH. Each monomere binds BH4 molecule as a cofactor which is shown here as spheres. The homo-tetrameric PAH has a two-fold symetry, which is drawn here as dashed black line (10).) (top)

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