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- PDB-1hpg: A glutamic acid specific serine protease utilizes a novel histidi... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1hpg | ||||||
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Title | A glutamic acid specific serine protease utilizes a novel histidine triad in substrate binding | ||||||
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![]() | HYDROLASE/HYDROLASE INHIBITOR / SERINE PROTEASE / HYDROLASE-HYDROLASE INHIBITOR COMPLEX | ||||||
Function / homology | ![]() glutamyl endopeptidase II / Hydrolases; Acting on peptide bonds (peptidases); Serine endopeptidases / serine-type endopeptidase activity / extracellular region Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() | ||||||
![]() | Nienaber, V.L. / Birktoft, J.J. | ||||||
![]() | ![]() Title: A glutamic acid specific serine protease utilizes a novel histidine triad in substrate binding. Authors: Nienaber, V.L. / Breddam, K. / Birktoft, J.J. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 45.7 KB | Display | ![]() |
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PDB format | ![]() | 34.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 367.1 KB | Display | ![]() |
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Full document | ![]() | 366.9 KB | Display | |
Data in XML | ![]() | 5.5 KB | Display | |
Data in CIF | ![]() | 8.7 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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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Atom site foot note | 1: SER A 79 - GLY A 80 OMEGA = 320.79 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION 2: CIS PROLINE - PRO A 99 |
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Components
#1: Protein | Mass: 18279.891 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() References: UniProt: Q54211, UniProt: Q07006*PLUS, glutamyl endopeptidase II |
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#2: Protein/peptide | |
#3: Water | ChemComp-HOH / |
Nonpolymer details | HOH 401 FITS THE CRITERIA OF A SODIUM ATOM BUT WAS REFINED AS AN ORDERED SOLVENT. |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 1.87 Å3/Da / Density % sol: 34.3 % | ||||||||||||||||||||||||||||||
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Crystal grow | *PLUS Temperature: 20 ℃ / pH: 7.5 / Method: vapor diffusion, sitting 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 | Resolution: 1.5→30 Å / Num. obs: 22913 / % possible obs: 94.4 % / Observed criterion σ(I): 2 |
Reflection | *PLUS Highest resolution: 1.8 Å / Num. all: 13006 / Num. measured all: 90655 / Rmerge(I) obs: 0.083 |
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Processing
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Refinement | Rfactor Rwork: 0.181 / Rfactor obs: 0.181 / Highest resolution: 1.5 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Highest resolution: 1.5 Å
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Refine LS restraints |
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Refinement | *PLUS Highest resolution: 2 Å / Rfactor obs: 0.17 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS Type: x_angle_deg / Dev ideal: 3.18 |