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Open data
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Basic information
Entry | Database: PDB / ID: 1gvx | |||||||||
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Title | Endothiapepsin complexed with H256 | |||||||||
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![]() | HYDROLASE/HYDROLASE INHIBITOR / HYDROLASE / ASPARTIC PROTEINASE MECHANISM / TETRAHEDRAL INTERMEDIATE / HYDROLASE-HYDROLASE INHIBITOR COMPLEX | |||||||||
Function / homology | ![]() | |||||||||
Biological species | ![]() SYNTHETIC CONSTRUCT (others) | |||||||||
Method | ![]() ![]() ![]() | |||||||||
![]() | Coates, L. / Erskine, P.T. / Crump, M.P. / Wood, S.P. / Cooper, J.B. | |||||||||
![]() | ![]() Title: Five Atomic Resolution Structures of Endothiapepsin Inhibitor Complexes: Implications for the Aspartic Proteinase Mechanism Authors: Coates, L. / Erskine, P.T. / Crump, M.P. / Wood, S.P. / Cooper, J.B. | |||||||||
History |
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Remark 700 | SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN ... SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW, TWO SHEETS ARE DEFINED. |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 152.5 KB | Display | ![]() |
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PDB format | ![]() | 119.1 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 382.2 KB | Display | ![]() |
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Full document | ![]() | 382.4 KB | Display | |
Data in XML | ![]() | 8.4 KB | Display | |
Data in CIF | ![]() | 15.1 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1gvtC ![]() 1gvuC ![]() 1gvvC ![]() 1gvwC ![]() 3er5S C: citing same article ( S: Starting model for refinement |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 33795.840 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() References: UniProt: P11838, endothiapepsin | ||
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#2: Protein/peptide | ![]() References: N-{(2R)-3-phenyl-2-[(L-prolyl-L-threonyl-L-alpha-glutamyl)amino]propyl}-L-phenylalanyl-N~5~-[amino(iminio)methyl]- L-ornithyl-L-glutamic acid | ||
#3: Chemical | #4: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.04 Å3/Da / Density % sol: 39.83 % | |||||||||||||||
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Crystal grow | pH: 4.5 / Details: PH 4.50 | |||||||||||||||
Crystal grow | *PLUS Method: unknown | |||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 130 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC CCD / Detector: CCD / Date: Apr 1, 2001 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.933 Å / Relative weight: 1 |
Reflection | Resolution: 1→10 Å / Num. obs: 136765 / % possible obs: 96.9 % / Redundancy: 6.9 % / Rmerge(I) obs: 0.079 / Net I/σ(I): 12.7 |
Reflection shell | Resolution: 1→1.05 Å / Redundancy: 6.1 % / Rmerge(I) obs: 0.163 / Mean I/σ(I) obs: 3.6 / % possible all: 94.3 |
Reflection | *PLUS Lowest resolution: 10 Å |
Reflection shell | *PLUS % possible obs: 94.3 % |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 3ER5 Resolution: 1→10 Å / Cross valid method: THROUGHOUT / σ(F): 0 / Stereochemistry target values: ENGH AND HUBER
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Solvent computation | Solvent model: MOEWS AND KRETSINGER | |||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1→10 Å
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Refine LS restraints |
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Refinement | *PLUS Lowest resolution: 10 Å / Rfactor Rfree: 0.1647 / Rfactor Rwork: 0.1393 | |||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | |||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS |