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Hydroxylases 3D structures

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Current revision (09:05, 31 May 2023) (edit) (undo)
 
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Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
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{{#tree:id=OrganizedByTopic|openlevels=0|
{{#tree:id=OrganizedByTopic|openlevels=0|
-
*Phenylalanine hydroxylase
+
 
 +
*Phenylalanine hydroxylase (cofactor tetrahydrobiopterin)
**[[6n1k]] – hPAH (mutant) – human<br />
**[[6n1k]] – hPAH (mutant) – human<br />
Line 14: Line 15:
**[[1j8u]] - hPAH catalytic domain + cofactor<br />
**[[1j8u]] - hPAH catalytic domain + cofactor<br />
**[[1dmw]] - hPAH catalytic domain + cofactor<br />
**[[1dmw]] - hPAH catalytic domain + cofactor<br />
-
**[[6hpo]] - hPAH catalytic domain + cofactor + Fe<br />
 
**[[1tg2]], [[1lrm]] - hPAH catalytic domain (mutant) + cofactor<br />
**[[1tg2]], [[1lrm]] - hPAH catalytic domain (mutant) + cofactor<br />
**[[1mmk]], [[1mmt]], [[1kw0]] - hPAH catalytic domain + cofactor + substrate<br />
**[[1mmk]], [[1mmt]], [[1kw0]] - hPAH catalytic domain + cofactor + substrate<br />
-
**[[4anp]] - hPAH catalytic domain + pyrimidine derivative<br />
+
**[[4anp]] - hPAH catalytic domain + pyrimidine derivative
**[[5fii]], [[5fgi]] - hPAH residues 19-118 + phenylalanine<br />
**[[5fii]], [[5fgi]] - hPAH residues 19-118 + phenylalanine<br />
**[[1phz]], [[2phm]], [[5den]], [[5fgj]], [[5den]] – rPAH - rat<br />
**[[1phz]], [[2phm]], [[5den]], [[5fgj]], [[5den]] – rPAH - rat<br />
Line 26: Line 26:
**[[2v27]], [[2v28]] – PAH – ''Colwellia psychrerythraea''<br />
**[[2v27]], [[2v28]] – PAH – ''Colwellia psychrerythraea''<br />
**[[1ltu]], [[1ltv]] – CvPAH – ''Chromobacterium violaceum''<br />
**[[1ltu]], [[1ltv]] – CvPAH – ''Chromobacterium violaceum''<br />
-
**[[1phz]], [[2phm]], [[5fgj]], [[5den]] – rPAH - rat<br />
+
**[[4bpt]] – PAH – ''Legionella pneumophila''<br />
-
**[[5egq]] - rPAH (mutant) <br />
+
-
**[[4bpt]] – PAH –'' Legionella pneumophila''<br />
+
**[[1ltz]] - CvPAH + cofactor<br />
**[[1ltz]] - CvPAH + cofactor<br />
**[[3tcy]], [[3tk2]] – CvPAH + phenylalanine<br />
**[[3tcy]], [[3tk2]] – CvPAH + phenylalanine<br />
Line 35: Line 33:
**[[4jpx]] - CvPAH (mutant) + Co + phenylalanine<br />
**[[4jpx]] - CvPAH (mutant) + Co + phenylalanine<br />
**[[4jpy]] - CvPAH + Fe + phenylalanine<br />
**[[4jpy]] - CvPAH + Fe + phenylalanine<br />
 +
**[[7vgm]] - PAH + Fe – ''Bacillus cereus''<br />
-
*Tyrosine hydroxylase
+
*Tyrosine hydroxylase (cofactor tetrahydrobiopterin)
-
**[[2xsn]] – hTH catalytic domain <br />
+
**[[7a2g]] – hTH – Cryo EM<br />
-
**[2toh]], [[1toh]] – TH catalytic and tetramerization domains - rat
+
**[[6zn2]], [[6zvp]], [[7pim]] – hTH + dopamine – Cryo EM<br />
 +
**[[2xsn]], [[6zzu]] – hTH catalytic domain 193-528<br />
 +
**[2toh]], [[1toh]] – rTH catalytic and tetramerization domains 160-498 – rat
 +
**[[2mda]] – rTH regulatory domain 65-159 – NMR<br />
 +
**[[7kqr]], [[7kqs]], [[7kqt]], [[7kqu]] – TH + heme + Tyr derivative – ''Streptomyces sclerotialus'' <br />
*Tryptophan hydroxylase
*Tryptophan hydroxylase
-
**[[3hf8]], [[3hfb]], [[3hf6]], [[5tpg]], [[5l01]], [[5j6d]] – hTPH 1 catalytic domain+ inhibitor + Fe <br />
+
**[[7wiy]] – hTPH 2 + Fe – Cryo EM<br />
 +
**[[3hf8]], [[3hfb]], [[3hf6]], [[5tpg]], [[5l01]], [[5j6d]], [[7zig]], [[7zih]], [[7zif]], [[7zii]], [[7zij]], [[7zik]] – hTPH 1 catalytic domain 105-401 + inhibitor + Fe <br />
**[[1mlw]] – hTPH catalytic domain+ biopterin + Fe<br />
**[[1mlw]] – hTPH catalytic domain+ biopterin + Fe<br />
**[[4v06]] - hTPH 2 catalytic domain + Fe<br />
**[[4v06]] - hTPH 2 catalytic domain + Fe<br />
 +
**[[7qri]] - hTPH 2 regulatory domain 48-145 + Phe - NMR<br />
**[[3e2t]] – TPH 1 catalytic domain + Trp + Fe – chicken
**[[3e2t]] – TPH 1 catalytic domain + Trp + Fe – chicken
Line 51: Line 56:
**[[1phh]] – PfPHBH + FAD + DHB – ''Pseudomonas fluorescens''<br />
**[[1phh]] – PfPHBH + FAD + DHB – ''Pseudomonas fluorescens''<br />
-
**[[1dob]], [[1doc]], [[1pxa]], [[1pxb]], [[1pxc]] – PaPHBH + FAD + PHB – ''Pseudomonas aeruginosa''<br />
 
**[[2phh]] – PfPHBH + adenosine diphosphoribose + PHB <br />
**[[2phh]] – PfPHBH + adenosine diphosphoribose + PHB <br />
**[[1pbb]] – PfPHBH + FAD + 2,4-DHB <br />
**[[1pbb]] – PfPHBH + FAD + 2,4-DHB <br />
Line 60: Line 64:
**[[1pdh]] – PfPHBH + FAD derivative + PHB <br />
**[[1pdh]] – PfPHBH + FAD derivative + PHB <br />
**[[1cj2]], [[1cj3]], [[1cj4]] – PfPHBH (mutant) + FAD derivative + PHB <br />
**[[1cj2]], [[1cj3]], [[1cj4]] – PfPHBH (mutant) + FAD derivative + PHB <br />
-
**[[1dod]], [[1doe]] – PaPHBH + FAD + 2,4-DHB <br />
+
**[[1dob]], [[1doc]], [[1pxa]], [[1pxb]], [[1pxc]] – PaPHBH + FAD + PHB – ''Pseudomonas aeruginosa''<br />
 +
**[[1dod]], [[1doe]], [[1iuv]], [[1iuw]], [[1iux]] – PaPHBH + FAD + DHB derivative<br />
**[[1ius]], [[1iut]], [[1iuu]] – PaPHBH + FAD + 4-aminobenzoate <br />
**[[1ius]], [[1iut]], [[1iuu]] – PaPHBH + FAD + 4-aminobenzoate <br />
-
**[[1iuv]], [[1iuw]], [[1iux]] – PaPHBH + FAD + 4,4-DHB <br />
+
**[[6ju1]] – PaPHBH (mutant) + FAD + DHB derivative <br />
**[[1d7l]] – PaPHBH + FAD derivative + PHB <br />
**[[1d7l]] – PaPHBH + FAD derivative + PHB <br />
**[[1k0i]], [[1ykj]] – PaPHBH (mutant) + FAD + PHB <br />
**[[1k0i]], [[1ykj]] – PaPHBH (mutant) + FAD + PHB <br />
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**[[2dkh]] – CtPHBH + FAD + hydroxy-benzoate <br />
**[[2dkh]] – CtPHBH + FAD + hydroxy-benzoate <br />
-
*Apartyl/asparaginyl β-hydroxylase
+
*Apartyl/asparaginyl b-hydroxylase; Domain – oxygenase and TPR 301-758
 +
**[[6qa5]] – hAAH oxygenase and TPR domain<br />
**[[5jz6]] – hAAH oxygenase and TPR domain + malate + Mn <br />
**[[5jz6]] – hAAH oxygenase and TPR domain + malate + Mn <br />
**[[5apa]] – hAAH residues 562-758 + malate + Ni <br />
**[[5apa]] – hAAH residues 562-758 + malate + Ni <br />
**[[5jza]] – hAAH oxygenase and TPR domain + oxalylglycine + Mn <br />
**[[5jza]] – hAAH oxygenase and TPR domain + oxalylglycine + Mn <br />
-
**[[5jz8]], [[5jzu]], [[6rk9]], [[5jqy]] – hAAH oxygenase and TPR domain + oxalylglycine + Mn + coagulation factor X peptide<br />
+
**[[6yyu]], [[6yyv]] – hAAH oxygenase and TPR domain + oxoglutarate + Mn <br />
-
**[[5jtc]] – hAAH oxygenase and TPR domain + pyridine dicarboxylate + Mn + coagulation factor X peptide<br />
+
**[[6yyw]], [[6yyx]], [[6yyy]], [[6z6q]] – hAAH oxygenase and TPR domain + oxoglutarate + Mn + coagulation factor X peptide<br />
 +
**[[5jz8]], [[5jzu]], [[6rk9]], [[5jqy]], [[6z6r]] – hAAH oxygenase and TPR domain + oxalyl derivative + Mn + coagulation factor X peptide<br />
 +
**[[7e6j]] – hAAH oxygenase and TPR domain (mutant) + coagulation factor X peptide<br />
 +
**[[6q9f]], [[6q9i]] – hAAH oxygenase and TPR domain (mutant) + oxalylglycine + Mn + coagulation factor X peptide<br />
 +
**[[5jtc]], [[7bmi]], [[7bmj]] – hAAH oxygenase and TPR domain + pyridine dicarboxylate + Mn + coagulation factor X peptide<br />
*Alpha-ketoglutarate-dependent L-arginine hydroxylase
*Alpha-ketoglutarate-dependent L-arginine hydroxylase
**[[6dax]], [[6alm]], [[6aln]], [[6mp8]] – SvAAH + arginine + oxoglutarate + Fe – ''Streptomyces vinaceus''<br />
**[[6dax]], [[6alm]], [[6aln]], [[6mp8]] – SvAAH + arginine + oxoglutarate + Fe – ''Streptomyces vinaceus''<br />
-
**[[6daz]], [[6alo]], [[6alp]], [[6alq]] – SvAAH + arginine + succinate + Fe <br />
+
**[[6daz]], [[6alo]], [[6alp]], [[6alq]], [[6y12]] – SvAAH + arginine + succinate + Fe <br />
 +
**[[6y0n]] – SvAAH + arginine + AKG + Fe <br />
**[[6db2]], [[6alr]] – SvAAH + homoarginine + succinate + V <br />
**[[6db2]], [[6alr]] – SvAAH + homoarginine + succinate + V <br />
**[[6mp9]] – SvAAH + guanidinopentanoate + succinate + Fe <br />
**[[6mp9]] – SvAAH + guanidinopentanoate + succinate + Fe <br />
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**[[2wbq]] – SvVIOC + Arg derivative<br />
**[[2wbq]] – SvVIOC + Arg derivative<br />
**[[2wbp]] – SvVIOC + Fe + succinate + Arg derivative<br />
**[[2wbp]] – SvVIOC + Fe + succinate + Arg derivative<br />
 +
**[[6daw]] – NAPI + Fe + Arg – ''Streptomyces lusitanus''<br />
*Prolyl 4-hydroxylase
*Prolyl 4-hydroxylase
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**[[4bt8]], [[2yq8]] - hPH a1 subunit collagen-binding domain<br />
**[[4bt8]], [[2yq8]] - hPH a1 subunit collagen-binding domain<br />
**[[1tjc]] - hPH a1 subunit collagen-binding domain (mutant)<br />
**[[1tjc]] - hPH a1 subunit collagen-binding domain (mutant)<br />
-
**[[4btb]], [[4bta]], [[4bt9]] - hPH a1 subunit + peptide<br />
+
**[[2v5f]], [[4btb]], [[4bta]], [[4bt9]] - hPH a1 subunit + peptide<br />
**[[6evl]] - hPH a2 subunit <br />
**[[6evl]] - hPH a2 subunit <br />
**[[6evm]], [[6evn]], [[6evo]], [[6evp]] - hPH a2 subunit + peptide<br />
**[[6evm]], [[6evn]], [[6evo]], [[6evp]] - hPH a2 subunit + peptide<br />
-
**[[5hv0]] - PH + Cd – ''Bacillus anthracis'' <br />
+
**[[3itq]], [[5hv0]] - BaPH – ''Bacillus anthracis'' <br />
 +
**[[5hv4]] - BaPH + ketoglutarate<br />
**[[5c5u]] - PcvPH + Mn – Paramecium chlorella virus <br />
**[[5c5u]] - PcvPH + Mn – Paramecium chlorella virus <br />
**[[5c5t]] - PcvPH + Mn + Zn <br />
**[[5c5t]] - PcvPH + Mn + Zn <br />
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**[[4p7w]] - RlPH + Co + proline<br />
**[[4p7w]] - RlPH + Co + proline<br />
**[[6iuq]] - PH + Fe – ''Phytophthora capsici''<br />
**[[6iuq]] - PH + Fe – ''Phytophthora capsici''<br />
-
**[[6ey1]] - TaPH + Mn – ''Trichoplax adhaerens''<br />
 
-
**[[6f0w]] - TaPH + Mn + hypoxia inducible factor + oxalylglycine <br />
 
**[[2v4a]], [[2jij]] - CrPH – ''Chlamydomonas reinhardtii'' <br />
**[[2v4a]], [[2jij]] - CrPH – ''Chlamydomonas reinhardtii'' <br />
**[[2jig]] - CrPH + Zn + pyridine derivative<br />
**[[2jig]] - CrPH + Zn + pyridine derivative<br />
 +
**[[3gze]] - CrPH + Zn + peptide<br />
-
*HIF prolyl hydroxylase or egl nine homolog See [[Prolyl hydroxylase domain]]
+
*HIF prolyl hydroxylase or egl nine homolog See [[Prolyl hydroxylase domain]]
*Lysine 4-hydroxylase
*Lysine 4-hydroxylase
Line 148: Line 160:
**[[6f6j]] – CaL3H + Fe + succinate + hydroxyl lysine <br />
**[[6f6j]] – CaL3H + Fe + succinate + hydroxyl lysine <br />
-
*Salicilate hydroxylase
+
*Salicylate hydroxylase
 +
**[[6bz5]] - PpSH <br />
**[[5evy]] - PpSH + FAD + salicilate <br />
**[[5evy]] - PpSH + FAD + salicilate <br />
 +
**[[7c8z]] - SH + Fe2S2 + Fe - ''Ralstonia'' <br />
-
*Dopamine β-hydroxylase
+
*Dopamine b-hydroxylase (cofactor ascorbic acid)
**[[4zel]] - hDH + Cu <br />
**[[4zel]] - hDH + Cu <br />
Line 158: Line 172:
*Ectoine hydroxylase
*Ectoine hydroxylase
-
**[[4q5o]] - DH + Fe + 5-hydroxyectoine – ''Sphingopyxis alaskensis'' <br />
+
**[[4mhr]] - SaEH – ''Sphingopyxis alaskensis'' <br />
 +
**[[4mhu]] - SaEH + Fe <br />
 +
**[[4q5o]] - SaEH + Fe + 5-hydroxyectoine <br />
 +
**[[4nmi]] - VsEH – ''Virgibacillus salexigens''<br />
 +
**[[3emr]] - VsEH + Fe <br />
 +
 
 +
*Hyoscyamine 6 b-hydroxylase
 +
 
 +
**[[6ttm]], [[6ttn]] - dHH + Ni + oxalylglycine + hyoscyamine – datura<br />
 +
**[[6tto]] - dHH + Ni + oxoglutaratee <br />
*Cytochrome P450 hydroxylase See [[Cytochrome P450 hydroxylase]]
*Cytochrome P450 hydroxylase See [[Cytochrome P450 hydroxylase]]
 +
 +
*Toluene/o-xylene monooxygenase hydroxylase See [[Monooxygenase]]
 +
 +
*Ornithine hydroxylase See [[Monooxygenase]]
 +
 +
*Methane monooxygenase hydroxylase See [[Methane monooxygenase]]
 +
 +
*Kynurenine 3-hydroxylase or KMOSee [[Monooxygenase]]
 +
 +
*Trans-3/4-proline hydroxylase H11 See [[Dioxygenase]]
}}
}}
[[Category:Topic Page]]
[[Category:Topic Page]]

Current revision

3D structures of hydroxylases

Updated on 31-May-2023

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Joel L. Sussman

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