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- PDB-1ppl: CRYSTALLOGRAPHIC ANALYSIS OF TRANSITION-STATE MIMICS BOUND TO PEN... -
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Basic information
Entry | Database: PDB / ID: 1ppl | ||||||
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Title | CRYSTALLOGRAPHIC ANALYSIS OF TRANSITION-STATE MIMICS BOUND TO PENICILLOPEPSIN: PHOSPHORUS-CONTAINING PEPTIDE ANALOGUES | ||||||
![]() | PENICILLOPEPSIN | ||||||
![]() | HYDROLASE/hydrolase inhibitor / ACID PROTEINASE / HYDROLASE-hydrolase inhibitor complex | ||||||
Function / homology | ![]() penicillopepsin / aspartic-type endopeptidase activity / proteolysis / extracellular region Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() | ||||||
![]() | Fraser, M.E. / James, M.N.G. | ||||||
![]() | ![]() Title: Crystallographic analysis of transition-state mimics bound to penicillopepsin: phosphorus-containing peptide analogues. Authors: Fraser, M.E. / Strynadka, N.C. / Bartlett, P.A. / Hanson, J.E. / James, M.N. #1: ![]() Title: Aspartic Proteinases and Their Catalytic Pathway Authors: James, M.N.G. / Sielecki, A.R. #2: ![]() Title: Stereochemical Analysis of Peptide Bond Hydrolysis Catalyzed by the Aspartic Proteinase Penicillopepsin Authors: James, M.N.G. / Sielecki, A.R. #3: ![]() Title: Structure and Refinement of Penicillopepsin at 1.8 Angstroms Resolution Authors: James, M.N.G. / Sielecki, A.R. #4: ![]() Title: Conformational Flexibility in the Active Sites of Aspartyl Proteinases Revealed by a Pepstatin Fragment Binding to Penicillopepsin Authors: James, M.N.G. / Sielecki, A. / Salituro, F. / Rich, D.H. / Hofmann, T. #5: ![]() Year: 1981 Title: The Tertiary Structure of Penicillopepsin. Towards a Catalytic Mechanism for Acid Proteases Authors: James, M.N.G. / Hsu, I-N. / Hofmann, T. / Sielecki, A.R. #6: ![]() Title: An X-Ray Crystallographic Approach to Enzyme Structure and Function Authors: James, M.N.G. #7: ![]() Title: Structural Evidence for Gene Duplication in the Evolution of the Acid Proteases Authors: Tang, J. / James, M.N.G. / Hsu, I.N. / Jenkins, J.A. / Blundell, T.L. #8: ![]() Title: Mechanism of Acid Protease Catalysis Based on the Crystal Structure of Penicillopepsin Authors: James, M.N.G. / Hsu, I.-N. / Delbaere, L.T.J. #9: ![]() Title: Penicillopepsin from Penicillium Janthinellum Crystal Structure at 2.8 Angstroms and Sequence Homology with Porcine Pepsin Authors: Hsu, I.-N. / Delbaere, L.T.J. / James, M.N.G. / Hofmann, T. #10: ![]() Title: Penicillopepsin. 2.8 Angstroms Structure, Active Site Conformation and Mechanistic Implications Authors: Hsu, I-N. / Delbaere, L.T.J. / James, M.N.G. / Hofmann, T. #11: ![]() Title: The Crystal Structure of Penicillopepsin at 6 Angstroms Resolution Authors: Hsu, I-N. / Hofmann, T. / Nyburg, S.C. / James, M.N.G. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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PDBx/mmCIF format | ![]() | 77.3 KB | Display | ![]() |
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PDB format | ![]() | 59.5 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
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Links
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Assembly
Deposited unit | ![]()
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1 |
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Unit cell |
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Atom site foot note | 1: RESIDUES 134 AND 315 ARE CIS PROLINES. | |||||||||
Components on special symmetry positions |
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Components
-Protein , 1 types, 1 molecules E
#1: Protein | Mass: 33468.809 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() |
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-Sugars , 2 types, 2 molecules ![](data/chem/img/MAN.gif)
![](data/chem/img/XYS.gif)
![](data/chem/img/XYS.gif)
#3: Sugar | ChemComp-MAN / |
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#4: Sugar | ChemComp-XYS / |
-Non-polymers , 3 types, 278 molecules ![](data/chem/img/1Z7.gif)
![](data/chem/img/SO4.gif)
![](data/chem/img/HOH.gif)
![](data/chem/img/SO4.gif)
![](data/chem/img/HOH.gif)
#2: Chemical | ChemComp-1Z7 / |
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#5: Chemical | ChemComp-SO4 / |
#6: Water | ChemComp-HOH / |
-Details
Nonpolymer details | THE INHIBITOR SUBCOMPONENT ZPH HAS A MODIFIED LEUCINE IN WHICH THE CO GROUP HAS BEEN REPLACED WITH ...THE INHIBITOR SUBCOMPONE |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 1.98 Å3/Da / Density % sol: 37.96 % | ||||||||||||||||||||||||
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Crystal grow | *PLUS Temperature: 18-22 ℃ / pH: 4.4 / Method: vapor diffusion, hanging drop | ||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Radiation | Scattering type: x-ray |
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Radiation wavelength | Relative weight: 1 |
Reflection | *PLUS Highest resolution: 1.7 Å / Lowest resolution: 60 Å / Num. all: 29601 / Num. obs: 26533 / Num. measured all: 88917 / Rmerge(I) obs: 0.06 |
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Processing
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Refinement | Rfactor Rwork: 0.148 / Rfactor obs: 0.148 / Highest resolution: 1.7 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Highest resolution: 1.7 Å
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Refine LS restraints |
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Software | *PLUS Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Highest resolution: 1.7 Å / Lowest resolution: 8 Å / Num. reflection obs: 24760 / σ(F): 3 / Rfactor obs: 0.148 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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