2cfi: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2cfi]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CFI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2CFI FirstGlance]. <br> | <table><tr><td colspan='2'>[[2cfi]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CFI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2CFI FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZZZ:6-FORMYLTETRAHYDROPTERIN'>ZZZ</scene>< | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZZZ:6-FORMYLTETRAHYDROPTERIN'>ZZZ</scene></td></tr> | ||
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2bw0|2bw0]], [[2cq8|2cq8]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2bw0|2bw0]], [[2cq8|2cq8]]</td></tr> | ||
<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Formyltetrahydrofolate_dehydrogenase Formyltetrahydrofolate dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.5.1.6 1.5.1.6] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Formyltetrahydrofolate_dehydrogenase Formyltetrahydrofolate dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.5.1.6 1.5.1.6] </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=2cfi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cfi OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2cfi RCSB], [http://www.ebi.ac.uk/pdbsum/2cfi 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=2cfi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cfi OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2cfi RCSB], [http://www.ebi.ac.uk/pdbsum/2cfi PDBsum]</span></td></tr> | ||
<table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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[[Category: Formyltetrahydrofolate dehydrogenase]] | [[Category: Formyltetrahydrofolate dehydrogenase]] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Arrowsmith, C | [[Category: Arrowsmith, C]] | ||
[[Category: Edwards, A | [[Category: Edwards, A]] | ||
[[Category: Ehn, M | [[Category: Ehn, M]] | ||
[[Category: Graslund, S | [[Category: Graslund, S]] | ||
[[Category: Hallberg, M | [[Category: Hallberg, M]] | ||
[[Category: Hammarstrom, M | [[Category: Hammarstrom, M]] | ||
[[Category: Kotenyova, T | [[Category: Kotenyova, T]] | ||
[[Category: Kursula, P | [[Category: Kursula, P]] | ||
[[Category: Nilsson-Ehle, P | [[Category: Nilsson-Ehle, P]] | ||
[[Category: Nordlund, P | [[Category: Nordlund, P]] | ||
[[Category: Ogg, D J | [[Category: Ogg, D J]] | ||
[[Category: Persson, C | [[Category: Persson, C]] | ||
[[Category: Sagemark, J | [[Category: Sagemark, J]] | ||
[[Category: Schuler, H | [[Category: Schuler, H]] | ||
[[Category: Stenmark, P | [[Category: Stenmark, P]] | ||
[[Category: Sundstrom, M | [[Category: Sundstrom, M]] | ||
[[Category: Thorsell, A | [[Category: Thorsell, A]] | ||
[[Category: Weigelt, J | [[Category: Weigelt, J]] | ||
[[Category: Folate binding]] | [[Category: Folate binding]] | ||
[[Category: Nadp]] | [[Category: Nadp]] | ||
Revision as of 20:50, 15 January 2015
THE HYDROLASE DOMAIN OF HUMAN 10-FTHFD IN COMPLEX WITH 6-FORMYLTETRAHYDROPTERINTHE HYDROLASE DOMAIN OF HUMAN 10-FTHFD IN COMPLEX WITH 6-FORMYLTETRAHYDROPTERIN
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed10-Formyltetrahydrofolate dehydrogenase is a ubiquitously expressed enzyme in the human body. It catalyses the formation of tetrahydrofolate and carbon dioxide from 10-formyltetrahydrofolate, thereby playing an important role in the human metabolism of one-carbon units. It is a two-domain protein in which the N-terminal domain hydrolyses 10-formyltetrahydrofolate into formate and tetrahydrofolate. The high-resolution crystal structure of the hydrolase domain from human 10-formyltetrahydrofolate dehydrogenase has been determined in the presence and absence of a substrate analogue. The structures reveal conformational changes of two loops upon ligand binding, while key active-site residues appear to be pre-organized for catalysis prior to substrate binding. Two water molecules in the structures mark the positions of key oxygen moieties in the catalytic reaction and reaction geometries are proposed based on the structural data. Structures of the hydrolase domain of human 10-formyltetrahydrofolate dehydrogenase and its complex with a substrate analogue.,Kursula P, Schuler H, Flodin S, Nilsson-Ehle P, Ogg DJ, Savitsky P, Nordlund P, Stenmark P Acta Crystallogr D Biol Crystallogr. 2006 Nov;62(Pt 11):1294-9. Epub 2006, Oct 18. PMID:17057331[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)
OCA- Formyltetrahydrofolate dehydrogenase
- Homo sapiens
- Arrowsmith, C
- Edwards, A
- Ehn, M
- Graslund, S
- Hallberg, M
- Hammarstrom, M
- Kotenyova, T
- Kursula, P
- Nilsson-Ehle, P
- Nordlund, P
- Ogg, D J
- Persson, C
- Sagemark, J
- Schuler, H
- Stenmark, P
- Sundstrom, M
- Thorsell, A
- Weigelt, J
- Folate binding
- Nadp
- One-carbon metabolism
- Oxidoreductase
- Phosphopantetheine
- Tetrahydrofolate