1pek
From Proteopedia
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| - | [[Image:1pek.jpg|left|200px]] | + | [[Image:1pek.jpg|left|200px]] |
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| - | '''STRUCTURE OF THE COMPLEX OF PROTEINASE K WITH A SUBSTRATE-ANALOGUE HEXA-PEPTIDE INHIBITOR AT 2.2 ANGSTROMS RESOLUTION''' | + | {{Structure |
| + | |PDB= 1pek |SIZE=350|CAPTION= <scene name='initialview01'>1pek</scene>, resolution 2.2Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/Peptidase_K Peptidase K], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.64 3.4.21.64] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''STRUCTURE OF THE COMPLEX OF PROTEINASE K WITH A SUBSTRATE-ANALOGUE HEXA-PEPTIDE INHIBITOR AT 2.2 ANGSTROMS RESOLUTION''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1PEK is a [ | + | 1PEK is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PEK OCA]. |
==Reference== | ==Reference== | ||
| - | Structure of the complex of proteinase K with a substrate analogue hexapeptide inhibitor at 2.2-A resolution., Betzel C, Singh TP, Visanji M, Peters K, Fittkau S, Saenger W, Wilson KS, J Biol Chem. 1993 Jul 25;268(21):15854-8. PMID:[http:// | + | Structure of the complex of proteinase K with a substrate analogue hexapeptide inhibitor at 2.2-A resolution., Betzel C, Singh TP, Visanji M, Peters K, Fittkau S, Saenger W, Wilson KS, J Biol Chem. 1993 Jul 25;268(21):15854-8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8340410 8340410] |
[[Category: Peptidase K]] | [[Category: Peptidase K]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: hydrolase]] | [[Category: hydrolase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:23:21 2008'' |
Revision as of 11:23, 20 March 2008
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| , resolution 2.2Å | |||||||
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| Activity: | Peptidase K, with EC number 3.4.21.64 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
STRUCTURE OF THE COMPLEX OF PROTEINASE K WITH A SUBSTRATE-ANALOGUE HEXA-PEPTIDE INHIBITOR AT 2.2 ANGSTROMS RESOLUTION
Overview
The crystal structure of a transition state/product complex formed by the interaction between proteinase K and the substrate analogue N-Ac-L-Pro-L-Ala-L-Pro-L-Phe-D-Ala-L-Ala-NH2 has been determined at a resolution of 2.2 A and refined to an R-factor of 0.165 for 12,725 reflections. The inhibitor forms a stable complex through a series of hydrogen bonds with protein atoms and water molecules. The inhibitor is hydrolyzed between Phe 4I and D-Ala5I (I indicates inhibitor). The two fragments are separated by a distance of 3.07 A between the carbonyl carbon and the main chain nitrogen. Both fragments remain bound to the protein. The N-terminal fragment occupies subsites S5 to S1, whereas the C-terminal part is bound in S1' and S2', the first time that electron density for a substrate analogue has been observed in the P1' and P2' sites of a subtilisin-like enzyme. The flexible segments of the substrate recognition sites Gly100-Tyr104 and Ser132-Gly136 move appreciably to accommodate the inhibitor. Biochemical results indicate an inhibition by this specifically designed peptide of 95%.
About this Structure
1PEK is a Single protein structure of sequence from [1]. Full crystallographic information is available from OCA.
Reference
Structure of the complex of proteinase K with a substrate analogue hexapeptide inhibitor at 2.2-A resolution., Betzel C, Singh TP, Visanji M, Peters K, Fittkau S, Saenger W, Wilson KS, J Biol Chem. 1993 Jul 25;268(21):15854-8. PMID:8340410
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