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Open data
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Basic information
Entry | Database: PDB / ID: 1ac1 | ||||||
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Title | DSBA MUTANT H32L | ||||||
![]() | DSBA | ||||||
![]() | DISULFIDE OXIDOREDUCTASE / THIOREDOXIN FOLD / 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 | ![]() | ||||||
![]() | Guddat, L.W. / Martin, J.L. | ||||||
![]() | ![]() Title: Structural analysis of three His32 mutants of DsbA: support for an electrostatic role of His32 in DsbA stability. Authors: Guddat, L.W. / Bardwell, J.C. / Glockshuber, R. / Huber-Wunderlich, M. / Zander, T. / Martin, J.L. #1: ![]() Title: The Uncharged Surface Features Surrounding the Active Site of Escherichia Coli Dsba are Conserved and are Implicated in Peptide Binding Authors: Guddat, L.W. / Bardwell, J.C. / Zander, T. / Martin, J.L. #2: ![]() Title: Crystal Structure of the Dsba Protein Required for Disulphide Bond Formation in Vivo Authors: Martin, J.L. / Bardwell, J.C. / Kuriyan, 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 | ![]() | 82.1 KB | Display | ![]() |
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PDB format | ![]() | 65.5 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 408.9 KB | Display | ![]() |
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Full document | ![]() | 409.4 KB | Display | |
Data in XML | ![]() | 9 KB | Display | |
Data in CIF | ![]() | 13.5 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1acvC ![]() 1fvjC ![]() 1fvkSC S: Starting model for refinement C: citing same article ( |
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Similar 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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Noncrystallographic symmetry (NCS) | NCS oper: (Code: given Matrix: (-0.962443, 0.133572, 0.236352), Vector: |
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Components
#1: Protein | Mass: 21130.035 Da / Num. of mol.: 2 / Mutation: H32L Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() #2: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.8 Å3/Da / Density % sol: 53.1 % | ||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | pH: 6.3 / Details: CACODYLATE PH 6.3 PEG 8K 25% | ||||||||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 21 ℃ / pH: 6.5 / Method: vapor diffusion, hanging drop / Details: Martin, J.L., (1993) J.Mol.Biol., 230, 1097. | ||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 290 K |
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Diffraction source | Source: ![]() |
Detector | Type: RIGAKU RAXIS IIC / Detector: IMAGE PLATE / Date: Sep 1, 1996 / Details: MIRRORS |
Radiation | Monochromator: NI FILTER / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2→50 Å / Num. obs: 28490 / % possible obs: 91.5 % / Observed criterion σ(I): 1 / Redundancy: 2.9 % / Biso Wilson estimate: 27.2 Å2 / Rmerge(I) obs: 0.081 / Net I/σ(I): 13.6 |
Reflection shell | Resolution: 2→2.07 Å / Redundancy: 2.83 % / Rmerge(I) obs: 0.298 / Mean I/σ(I) obs: 2.36 / % possible all: 83 |
Reflection | *PLUS Num. measured all: 84044 |
Reflection shell | *PLUS Highest resolution: 2 Å / % possible obs: 83 % |
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Processing
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Refinement | Method to determine structure: DIFFERENCE FOURIER Starting model: 1.7 A STRUCTURE OF WILDTYPE OXIDISED DSBA (PDB ENTRY 1FVK) Resolution: 2→50 Å / Data cutoff low absF: 0.1 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 1 Details: BULK SOLVENT CORRECTION USED SOLDEN=0.34, SOLRAD = 0.25 A
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Displacement parameters | Biso mean: 33.5 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 2→50 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2→2.09 Å / Total num. of bins used: 8
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Xplor file |
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Software | *PLUS Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Rfactor Rfree: 0.22 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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