This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
3b7s
From Proteopedia
(New page: '''Unreleased structure''' The entry 3b7s is ON HOLD until Paper Publication Authors: Tholander, F., Haeggstrom, J., Thunnissen, M., Muroya, A., Roques, B.-P., Fournie-Zaluski, M.-C. D...) |
|||
| Line 1: | Line 1: | ||
| - | + | {{Seed}} | |
| + | [[Image:3b7s.jpg|left|200px]] | ||
| - | The | + | <!-- |
| + | The line below this paragraph, containing "STRUCTURE_3b7s", creates the "Structure Box" on the page. | ||
| + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | ||
| + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | ||
| + | or leave the SCENE parameter empty for the default display. | ||
| + | --> | ||
| + | {{STRUCTURE_3b7s| PDB=3b7s | SCENE= }} | ||
| - | + | ===[E296Q]LTA4H in complex with RSR substrate=== | |
| - | Description: [E296Q]LTA4H in complex with RSR substrate | ||
| + | <!-- | ||
| + | The line below this paragraph, {{ABSTRACT_PUBMED_17357161}}, adds the Publication Abstract to the page | ||
| + | (as it appears on PubMed at http://www.pubmed.gov), where 17357161 is the PubMed ID number. | ||
| + | --> | ||
| + | {{ABSTRACT_PUBMED_17357161}} | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed | + | ==About this Structure== |
| + | 3B7S is a [[Single protein]] structure of 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=3B7S OCA]. | ||
| + | |||
| + | ==Reference== | ||
| + | Assay for rapid analysis of the tri-peptidase activity of LTA4 hydrolase., Tholander F, Haeggstrom JZ, Proteins. 2007 Jun 1;67(4):1113-8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17357161 17357161] | ||
| + | |||
| + | Leukotriene A4 hydrolase: identification of a common carboxylate recognition site for the epoxide hydrolase and aminopeptidase substrates., Rudberg PC, Tholander F, Andberg M, Thunnissen MM, Haeggstrom JZ, J Biol Chem. 2004 Jun 25;279(26):27376-82. Epub 2004 Apr 12. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15078870 15078870] | ||
| + | |||
| + | Leukotriene A4 hydrolase/aminopeptidase. Glutamate 271 is a catalytic residue with specific roles in two distinct enzyme mechanisms., Rudberg PC, Tholander F, Thunnissen MM, Haeggstrom JZ, J Biol Chem. 2002 Jan 11;277(2):1398-404. Epub 2001 Oct 23. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11675384 11675384] | ||
| + | |||
| + | Leukotriene A4 hydrolase: selective abrogation of leukotriene B4 formation by mutation of aspartic acid 375., Rudberg PC, Tholander F, Thunnissen MM, Samuelsson B, Haeggstrom JZ, Proc Natl Acad Sci U S A. 2002 Apr 2;99(7):4215-20. Epub 2002 Mar 26. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11917124 11917124] | ||
| + | |||
| + | Crystal structure of human leukotriene A(4) hydrolase, a bifunctional enzyme in inflammation., Thunnissen MM, Nordlund P, Haeggstrom JZ, Nat Struct Biol. 2001 Feb;8(2):131-5. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11175901 11175901] | ||
| + | [[Category: Homo sapiens]] | ||
| + | [[Category: Single protein]] | ||
| + | [[Category: Fournie-Zaluski, M C.]] | ||
| + | [[Category: Haeggstrom, J.]] | ||
| + | [[Category: Muroya, A.]] | ||
| + | [[Category: Roques, B P.]] | ||
| + | [[Category: Tholander, F.]] | ||
| + | [[Category: Thunnissen, M.]] | ||
| + | [[Category: Alternative splicing]] | ||
| + | [[Category: Analogue peptide]] | ||
| + | [[Category: Cytoplasm]] | ||
| + | [[Category: Hydrolase]] | ||
| + | [[Category: Hydrolysis]] | ||
| + | [[Category: Leukotriene biosynthesis]] | ||
| + | [[Category: Metal-binding]] | ||
| + | [[Category: Metalloprotease]] | ||
| + | [[Category: Multifunctional enzyme]] | ||
| + | [[Category: Protease]] | ||
| + | [[Category: Transition state]] | ||
| + | [[Category: Tripeptide substrate]] | ||
| + | [[Category: Zinc]] | ||
| + | |||
| + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Sep 17 14:23:32 2008'' | ||
Revision as of 11:23, 17 September 2008
[E296Q]LTA4H in complex with RSR substrate
Template:ABSTRACT PUBMED 17357161
About this Structure
3B7S is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Assay for rapid analysis of the tri-peptidase activity of LTA4 hydrolase., Tholander F, Haeggstrom JZ, Proteins. 2007 Jun 1;67(4):1113-8. PMID:17357161
Leukotriene A4 hydrolase: identification of a common carboxylate recognition site for the epoxide hydrolase and aminopeptidase substrates., Rudberg PC, Tholander F, Andberg M, Thunnissen MM, Haeggstrom JZ, J Biol Chem. 2004 Jun 25;279(26):27376-82. Epub 2004 Apr 12. PMID:15078870
Leukotriene A4 hydrolase/aminopeptidase. Glutamate 271 is a catalytic residue with specific roles in two distinct enzyme mechanisms., Rudberg PC, Tholander F, Thunnissen MM, Haeggstrom JZ, J Biol Chem. 2002 Jan 11;277(2):1398-404. Epub 2001 Oct 23. PMID:11675384
Leukotriene A4 hydrolase: selective abrogation of leukotriene B4 formation by mutation of aspartic acid 375., Rudberg PC, Tholander F, Thunnissen MM, Samuelsson B, Haeggstrom JZ, Proc Natl Acad Sci U S A. 2002 Apr 2;99(7):4215-20. Epub 2002 Mar 26. PMID:11917124
Crystal structure of human leukotriene A(4) hydrolase, a bifunctional enzyme in inflammation., Thunnissen MM, Nordlund P, Haeggstrom JZ, Nat Struct Biol. 2001 Feb;8(2):131-5. PMID:11175901
Page seeded by OCA on Wed Sep 17 14:23:32 2008
Categories: Homo sapiens | Single protein | Fournie-Zaluski, M C. | Haeggstrom, J. | Muroya, A. | Roques, B P. | Tholander, F. | Thunnissen, M. | Alternative splicing | Analogue peptide | Cytoplasm | Hydrolase | Hydrolysis | Leukotriene biosynthesis | Metal-binding | Metalloprotease | Multifunctional enzyme | Protease | Transition state | Tripeptide substrate | Zinc
