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- PDB-1bq7: DSBA MUTANT P151A, ROLE OF THE CIS-PROLINE IN THE ACTIVE SITE OF DSBA -
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Open data
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Basic information
Entry | Database: PDB / ID: 1bq7 | ||||||
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Title | DSBA MUTANT P151A, ROLE OF THE CIS-PROLINE IN THE ACTIVE SITE OF DSBA | ||||||
![]() | PROTEIN (DISULFIDE OXIDOREDUCTASE) | ||||||
![]() | OXIDOREDUCTASE / DISULFIDE OXIDOREDUCTASE / PROTEIN DISULFIDE ISOMERASE / PROTEIN FOLDING / REDOX PROTEIN / REDOX-ACTIVE CENTER | ||||||
Function / homology | ![]() cellular response to antibiotic / protein disulfide isomerase activity / protein-disulfide reductase activity / outer membrane-bounded periplasmic space / periplasmic space / oxidoreductase activity Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Charbonnier, J.-B. / Stura, E.A. | ||||||
![]() | ![]() Title: On the role of the cis-proline residue in the active site of DsbA. Authors: Charbonnier, J.B. / Belin, P. / Moutiez, M. / Stura, E.A. / Quemeneur, E. #1: ![]() Title: Structural Analysis of Three His32 Mutants of DsbA: Support for an Electrostatic Role of His32 in DsbA Stability Authors: Guddat, L. / Bardwell, J.C. / Glockshuber, R. / Huber-Wunderlich, M. / Zander, T. / Martin, J.L. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 198.9 KB | Display | ![]() |
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PDB format | ![]() | 164.3 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 394.6 KB | Display | ![]() |
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Full document | ![]() | 420.7 KB | Display | |
Data in XML | ![]() | 23.9 KB | Display | |
Data in CIF | ![]() | 36.3 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1fvkS 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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Noncrystallographic symmetry (NCS) | NCS domain:
NCS oper:
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Components
#1: Protein | Mass: 21128.988 Da / Num. of mol.: 6 / Mutation: P151A Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() Compound details | THERE ARE SIX MOLECULES IN THE ASYMMETRIC UNIT. EACH CONTAINS 186 RESIDUES THE ACTIVE SITE ...THERE ARE SIX MOLECULES IN THE ASYMMETRIC | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.05 Å3/Da / Density % sol: 59.51 % | ||||||||||||||||||||||||||||||||||||||||
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Crystal grow | pH: 6.5 Details: 25% PEG 8,000 100 MM NACL 100 MM SODIUM CACODYLATE, PH 6.5 10% DMSO DIFFUSION VAPOR AT ROOM TEMPERATURE, SEEDING | ||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 21 ℃ / Method: vapor diffusion, hanging drop | ||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 289 K |
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Diffraction source | Source: ![]() ![]() |
Detector | Date: Jul 15, 1997 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.97 Å / Relative weight: 1 |
Reflection | Resolution: 2.8→20 Å / Num. obs: 31364 / % possible obs: 84.6 % / Observed criterion σ(I): 0.3 / Redundancy: 3.8 % / Rmerge(I) obs: 0.078 / Rsym value: 0.078 / Net I/σ(I): 13.3 |
Reflection shell | Resolution: 2.8→2.9 Å / Rmerge(I) obs: 0.475 / Mean I/σ(I) obs: 2.3 / Rsym value: 0.475 / % possible all: 87.7 |
Reflection | *PLUS Num. measured all: 117916 |
Reflection shell | *PLUS % possible obs: 87.9 % / Mean I/σ(I) obs: 1.7 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 1FVK Resolution: 2.8→10 Å / Cross valid method: THROUGHOUT / σ(F): 1 Details: PRO 151 IS MUTATED TO ALANINE. PEPTIDE BOND VAL150-PRO151 IS IN CIS CONFORMATION IN WILD TYPE DSBA. IT IS IN TRANS-CONFORMATION IN MUTANT DSBA PRO 151 ALA.
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Displacement parameters | Biso mean: 53.7 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.8→10 Å
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Refine LS restraints |
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Refine LS restraints NCS |
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LS refinement shell | Resolution: 2.8→2.92 Å
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Software | *PLUS Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Highest resolution: 2.8 Å / σ(F): 1 / % reflection Rfree: 5 % | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS Biso mean: 53.7 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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LS refinement shell | *PLUS Highest resolution: 2.8 Å / Rfactor Rfree: 0.418 / % reflection Rfree: 4.5 % / Rfactor Rwork: 0.348 |