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Prolyl hydroxylase domain

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== 3D Structures of prolyl hydroxylase domain ==
== 3D Structures of prolyl hydroxylase domain ==
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[[2y33]] – hPHD2 catalytic domain + Zn + chloro-iodoisoquinolin-carbonyl glycine – human<br />
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[[2y34]] - hPHD2 catalytic domain + Fe + chloro-iodoisoquinolin-carbonyl glycine<br />
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[[3ouh]], [[3oui]] - hPHD2 catalytic domain + Fe + inhibitor<br />
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[[3ouj]] - hPHD2 catalytic domain + Fe + 2OG<br />
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[[3hqr]] - hPHD2 catalytic domain (mutant) + Mn + HIF 1 α C terminal + oxalylglycine<br />
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[[3hqu]] - hPHD2 catalytic domain + Fe + HIF 1 α C terminal + chloro-iodoisoquinolin-carbonyl glycine<br />
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[[2hbt]], [[2hbu]] - hPHD2 catalytic domain + Fe + chloro-iodoisoquinolin-carbonyl glycine<br />
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[[2g19]], [[2g1m]] - hPHD2 catalytic domain + Fe + hydroxy-iodoisoquinolin-carbonyl glycine<br />
[[Category:Topic Page]]
[[Category:Topic Page]]

Revision as of 09:27, 27 July 2011

Template:STRUCTURE 3hqu

Prolyl hydroxylase domain (PHD) proteins mediate oxygen-dependent degradation of Hypoxia-inducible factor (HIF) α subunit. They include PHD1, PHD2 and PHD3. The PHD is a Fe+2/oxogluterate (2OG)-dependent enzyme. For more detalis see Molecular Playground/Prolyl Hydroxylase Domain (PHD) Enzyme.

Contents

3D Structures of prolyl hydroxylase domain

2y33 – hPHD2 catalytic domain + Zn + chloro-iodoisoquinolin-carbonyl glycine – human
2y34 - hPHD2 catalytic domain + Fe + chloro-iodoisoquinolin-carbonyl glycine
3ouh, 3oui - hPHD2 catalytic domain + Fe + inhibitor
3ouj - hPHD2 catalytic domain + Fe + 2OG
3hqr - hPHD2 catalytic domain (mutant) + Mn + HIF 1 α C terminal + oxalylglycine
3hqu - hPHD2 catalytic domain + Fe + HIF 1 α C terminal + chloro-iodoisoquinolin-carbonyl glycine
2hbt, 2hbu - hPHD2 catalytic domain + Fe + chloro-iodoisoquinolin-carbonyl glycine
2g19, 2g1m - hPHD2 catalytic domain + Fe + hydroxy-iodoisoquinolin-carbonyl glycine

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky, Joel L. Sussman

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