1lhd: Difference between revisions

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[[Image:1lhd.gif|left|200px]]<br /><applet load="1lhd" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:1lhd.gif|left|200px]]
caption="1lhd, resolution 2.35&Aring;" />
 
'''HUMAN ALPHA-THROMBIN COMPLEXED WITH AC-(D)PHE-PRO-BOROLYS-OH'''<br />
{{Structure
|PDB= 1lhd |SIZE=350|CAPTION= <scene name='initialview01'>1lhd</scene>, resolution 2.35&Aring;
|SITE=
|LIGAND= <scene name='pdbligand=DI2:AC-(D)PHE-PRO-BOROLYS-OH'>DI2</scene>
|ACTIVITY= [http://en.wikipedia.org/wiki/Thrombin Thrombin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.5 3.4.21.5]
|GENE=
}}
 
'''HUMAN ALPHA-THROMBIN COMPLEXED WITH AC-(D)PHE-PRO-BOROLYS-OH'''
 


==Overview==
==Overview==
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==About this Structure==
==About this Structure==
1LHD is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Hirudo_medicinalis Hirudo medicinalis] and [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=DI2:'>DI2</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Thrombin Thrombin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.5 3.4.21.5] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LHD OCA].  
1LHD is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Hirudo_medicinalis Hirudo medicinalis] and [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LHD OCA].  


==Reference==
==Reference==
Kinetic and crystallographic studies of thrombin with Ac-(D)Phe-Pro-boroArg-OH and its lysine, amidine, homolysine, and ornithine analogs., Weber PC, Lee SL, Lewandowski FA, Schadt MC, Chang CW, Kettner CA, Biochemistry. 1995 Mar 21;34(11):3750-7. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=7893672 7893672]
Kinetic and crystallographic studies of thrombin with Ac-(D)Phe-Pro-boroArg-OH and its lysine, amidine, homolysine, and ornithine analogs., Weber PC, Lee SL, Lewandowski FA, Schadt MC, Chang CW, Kettner CA, Biochemistry. 1995 Mar 21;34(11):3750-7. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/7893672 7893672]
[[Category: Hirudo medicinalis]]
[[Category: Hirudo medicinalis]]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: zymogen]]
[[Category: zymogen]]


''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:45:00 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:30:50 2008''

Revision as of 13:30, 20 March 2008

File:1lhd.gif


PDB ID 1lhd

Drag the structure with the mouse to rotate
, resolution 2.35Å
Ligands:
Activity: Thrombin, with EC number 3.4.21.5
Coordinates: save as pdb, mmCIF, xml



HUMAN ALPHA-THROMBIN COMPLEXED WITH AC-(D)PHE-PRO-BOROLYS-OH


OverviewOverview

The X-ray crystallographic structure of Ac-(D)Phe-Pro-boroArg-OH [DuP714, Ki = 0.04 nM; Kettner, C., Mersinger, L., & Knabb, R. (1990) J. Biol. Chem. 265, 18289] complexed with human alpha-thrombin shows the boron atom covalently bonded to the side-chain oxygen of the active site serine, Ser195. The boron adopts a nearly tetrahedral geometry, and the boronic acid forms a set of interactions with the protein that mimic the tetrahedral transition state of serine proteases. Contributions of the arginine side chain to inhibitor affinity were examined by synthesis of the ornithine, lysine, homolysine, and amidine analogs of DuP714. The basic groups interact with backbone carbonyl groups, water molecules, and an aspartic acid side chain (Asp189) located in the thrombin S1 specificity pocket. The variation in inhibition constant by 3 orders of magnitude appears to reflect differences in the energetics of interactions made with thrombin and differences in ligand flexibility in solution.(ABSTRACT TRUNCATED AT 250 WORDS)

DiseaseDisease

Known diseases associated with this structure: Dysprothrombinemia OMIM:[176930], Hyperprothrombinemia OMIM:[176930], Hypoprothrombinemia OMIM:[176930]

About this StructureAbout this Structure

1LHD is a Protein complex structure of sequences from Hirudo medicinalis and Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

Kinetic and crystallographic studies of thrombin with Ac-(D)Phe-Pro-boroArg-OH and its lysine, amidine, homolysine, and ornithine analogs., Weber PC, Lee SL, Lewandowski FA, Schadt MC, Chang CW, Kettner CA, Biochemistry. 1995 Mar 21;34(11):3750-7. PMID:7893672

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