1qrp
From Proteopedia
| Line 4: | Line 4: | ||
|PDB= 1qrp |SIZE=350|CAPTION= <scene name='initialview01'>1qrp</scene>, resolution 1.96Å | |PDB= 1qrp |SIZE=350|CAPTION= <scene name='initialview01'>1qrp</scene>, resolution 1.96Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=CH3:METHYL GROUP'>CH3</scene> | + | |LIGAND= <scene name='pdbligand=CH3:METHYL+GROUP'>CH3</scene>, <scene name='pdbligand=HFA:ALPHA-HYDROXY-BETA-PHENYL-PROPIONIC+ACID'>HFA</scene>, <scene name='pdbligand=IVA:ISOVALERIC+ACID'>IVA</scene>, <scene name='pdbligand=PLE:LEUCINE+PHOSPHINIC+ACID'>PLE</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1qrp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qrp OCA], [http://www.ebi.ac.uk/pdbsum/1qrp PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1qrp RCSB]</span> | ||
}} | }} | ||
| Line 28: | Line 31: | ||
[[Category: James, M N.G.]] | [[Category: James, M N.G.]] | ||
[[Category: Tarasova, N I.]] | [[Category: Tarasova, N I.]] | ||
| - | [[Category: CH3]] | ||
[[Category: aspartic proteinase]] | [[Category: aspartic proteinase]] | ||
[[Category: phosphonate inhibitor]] | [[Category: phosphonate inhibitor]] | ||
[[Category: transition state analogue]] | [[Category: transition state analogue]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:18:02 2008'' |
Revision as of 20:18, 30 March 2008
| |||||||
| , resolution 1.96Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
HUMAN PEPSIN 3A IN COMPLEX WITH A PHOSPHONATE INHIBITOR IVA-VAL-VAL-LEU(P)-(O) PHE-ALA-ALA-OME
Overview
The refined crystal structure of the complex between human pepsin and a synthetic phosphonate inhibitor, Iva-Val-Val-Leu(P)-(O)Phe-Ala-Ala-OMe [Iva = isovaleryl, Leu(P) = the phosphinic acid analog of L-leucine, (O)Phe = L-3-phenyllactic acid, OMe = methyl ester], is presented. The structure was refined using diffraction data between 30 and 1.96 A resolution to a final R factor ( summation operator| |F(o)| - |F(c)| | / summation operator|F(o)|, where |F(o)| and |F(c)| are the observed and calculated structure-factor amplitudes, respectively) of 20.0%. The interactions of the inhibitor with the enzyme show the locations of the binding sites on the enzyme from S4 to S3'. Modeling of the inhibitor binding to porcine pepsin shows very similar binding sites, except at S4. Comparison of the complex structure with the structures of related inhibitors bound to penicillopepsin helps to rationalize the observed differences in the binding constants. The convergence of reaction mechanisms and geometries in different families of proteinases is also discussed.
About this Structure
1QRP is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structural study of the complex between human pepsin and a phosphorus-containing peptidic -transition-state analog., Fujinaga M, Cherney MM, Tarasova NI, Bartlett PA, Hanson JE, James MN, Acta Crystallogr D Biol Crystallogr. 2000 Mar;56(Pt 3):272-9. PMID:10713513
Page seeded by OCA on Sun Mar 30 23:18:02 2008
