2zpf
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2zpf]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Rhodococcus_erythropolis Rhodococcus erythropolis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZPF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ZPF FirstGlance]. <br> | <table><tr><td colspan='2'>[[2zpf]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Rhodococcus_erythropolis Rhodococcus erythropolis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZPF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ZPF FirstGlance]. <br> | ||
| - | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NO:NITRIC+OXIDE'>NO</scene>, <scene name='pdbligand=TB0:TERT-BUTYL+ISOCYANIDE'>TB0</scene>< | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NO:NITRIC+OXIDE'>NO</scene>, <scene name='pdbligand=TB0:TERT-BUTYL+ISOCYANIDE'>TB0</scene></td></tr> |
| - | <tr><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CSD:3-SULFINOALANINE'>CSD</scene>, <scene name='pdbligand=CSO:S-HYDROXYCYSTEINE'>CSO</scene></td></tr> | + | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CSD:3-SULFINOALANINE'>CSD</scene>, <scene name='pdbligand=CSO:S-HYDROXYCYSTEINE'>CSO</scene></td></tr> |
| - | <tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2ahj|2ahj]], [[2cz6|2cz6]], [[2cz7|2cz7]], [[2d0q|2d0q]], [[2zpb|2zpb]], [[2zpe|2zpe]], [[2zpg|2zpg]], [[2zph|2zph]], [[2zpi|2zpi]]</td></tr> | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2ahj|2ahj]], [[2cz6|2cz6]], [[2cz7|2cz7]], [[2d0q|2d0q]], [[2zpb|2zpb]], [[2zpe|2zpe]], [[2zpg|2zpg]], [[2zph|2zph]], [[2zpi|2zpi]]</td></tr> |
| - | <tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Nitrile_hydratase Nitrile hydratase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.84 4.2.1.84] </span></td></tr> | + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Nitrile_hydratase Nitrile hydratase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.84 4.2.1.84] </span></td></tr> |
| - | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2zpf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zpf OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2zpf RCSB], [http://www.ebi.ac.uk/pdbsum/2zpf PDBsum]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2zpf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zpf OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2zpf RCSB], [http://www.ebi.ac.uk/pdbsum/2zpf PDBsum]</span></td></tr> |
| - | <table> | + | </table> |
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/NHAA_RHOER NHAA_RHOER]] NHase catalyzes the hydration of various nitrile compounds to the corresponding amides. Industrial production of acrylamide is now being developed using some of the enzymes of this class. [[http://www.uniprot.org/uniprot/NHAB_RHOER NHAB_RHOER]] NHase catalyzes the hydration of various nitrile compounds to the corresponding amides. | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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[[Category: Nitrile hydratase]] | [[Category: Nitrile hydratase]] | ||
[[Category: Rhodococcus erythropolis]] | [[Category: Rhodococcus erythropolis]] | ||
| - | [[Category: Hashimoto, K | + | [[Category: Hashimoto, K]] |
| - | [[Category: Noguchi, T | + | [[Category: Noguchi, T]] |
| - | [[Category: Odaka, M | + | [[Category: Odaka, M]] |
| - | [[Category: Suzuki, H | + | [[Category: Suzuki, H]] |
| - | [[Category: Taniguchi, K | + | [[Category: Taniguchi, K]] |
| - | [[Category: Yohda, M | + | [[Category: Yohda, M]] |
[[Category: Iron]] | [[Category: Iron]] | ||
[[Category: Lyase]] | [[Category: Lyase]] | ||
[[Category: Metal-binding]] | [[Category: Metal-binding]] | ||
[[Category: Oxidation]] | [[Category: Oxidation]] | ||
Revision as of 05:12, 25 December 2014
Complex of Fe-type nitrile hydratase with tert-butylisonitrile, photo-activated for 18min at 293K
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