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2r99
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2r99]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1zcx 1zcx]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2R99 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2R99 FirstGlance]. <br> | <table><tr><td colspan='2'>[[2r99]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1zcx 1zcx]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2R99 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2R99 FirstGlance]. <br> | ||
| - | </td></tr><tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PPIE, CYP33 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr> | + | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PPIE, CYP33 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr> |
| - | <tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Peptidylprolyl_isomerase Peptidylprolyl isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.2.1.8 5.2.1.8] </span></td></tr> | + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Peptidylprolyl_isomerase Peptidylprolyl isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.2.1.8 5.2.1.8] </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=2r99 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2r99 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2r99 RCSB], [http://www.ebi.ac.uk/pdbsum/2r99 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=2r99 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2r99 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2r99 RCSB], [http://www.ebi.ac.uk/pdbsum/2r99 PDBsum]</span></td></tr> |
| - | <table> | + | </table> |
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/PPIE_HUMAN PPIE_HUMAN]] PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Combines RNA-binding and PPIase activities. May be involved in muscle- and brain-specific processes. May be involved in pre-mRNA splicing. | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Peptidylprolyl isomerase]] | [[Category: Peptidylprolyl isomerase]] | ||
| - | [[Category: Arrowsmith, C H | + | [[Category: Arrowsmith, C H]] |
| - | [[Category: Bochkarev, A | + | [[Category: Bochkarev, A]] |
| - | [[Category: Davis, T | + | [[Category: Davis, T]] |
| - | [[Category: Dhe-Paganon, S | + | [[Category: Dhe-Paganon, S]] |
| - | [[Category: Edwards, A M | + | [[Category: Edwards, A M]] |
| - | [[Category: Mackenzie, F | + | [[Category: Mackenzie, F]] |
| - | [[Category: Newman, E M | + | [[Category: Newman, E M]] |
| - | [[Category: | + | [[Category: Structural genomic]] |
| - | [[Category: Sundstrom, M | + | [[Category: Sundstrom, M]] |
| - | [[Category: Walker, J R | + | [[Category: Walker, J R]] |
[[Category: Cis-trans isomerization]] | [[Category: Cis-trans isomerization]] | ||
[[Category: Isomerase]] | [[Category: Isomerase]] | ||
| Line 43: | Line 45: | ||
[[Category: Sgc]] | [[Category: Sgc]] | ||
[[Category: Spliceosome]] | [[Category: Spliceosome]] | ||
| - | [[Category: Structural genomics consortium]] | ||
Revision as of 17:50, 24 December 2014
Crystal structure of cyclophilin ABH-like domain of human peptidylprolyl isomerase E isoform 1
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Categories: Homo sapiens | Peptidylprolyl isomerase | Arrowsmith, C H | Bochkarev, A | Davis, T | Dhe-Paganon, S | Edwards, A M | Mackenzie, F | Newman, E M | Structural genomic | Sundstrom, M | Walker, J R | Cis-trans isomerization | Isomerase | Mrna processing | Mrna splicing | Nucleus | Rna-binding | Rotamase | Sgc | Spliceosome
