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Yorodumi- PDB-1dsb: CRYSTAL STRUCTURE OF THE DSBA PROTEIN REQUIRED FOR DISULPHIDE BON... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1dsb | ||||||
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Title | CRYSTAL STRUCTURE OF THE DSBA PROTEIN REQUIRED FOR DISULPHIDE BOND FORMATION IN VIVO | ||||||
Components | DSBA | ||||||
Keywords | DISULFIDE OXIDOREDUCTASE | ||||||
Function / homology | Function and homology information 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 | Escherichia coli (E. coli) | ||||||
Method | X-RAY DIFFRACTION / Resolution: 2 Å | ||||||
Authors | Martin, J.L. / Bardwell, J.C.A. / Kuriyan, J. | ||||||
Citation | Journal: Nature / Year: 1993 Title: Crystal structure of the DsbA protein required for disulphide bond formation in vivo. Authors: Martin, J.L. / Bardwell, J.C. / Kuriyan, J. #1: Journal: J.Mol.Biol. / Year: 1993 Title: Crystallization of Dsba, an Escherichia Coli Protein Required for Disulphide Bond Formation in Vivo Authors: Martin, J.L. / Waksman, G. / Bardwell, J.C.A. / Beckwith, J. / Kuriyan, J. | ||||||
History |
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Remark 650 | HELIX HELIX A1' IS SEPARATED FROM A1 BY A THREE RESIDUE LOOP. HELIX B1' IS SEPARATED FROM B1 BY A ...HELIX HELIX A1' IS SEPARATED FROM A1 BY A THREE RESIDUE LOOP. HELIX B1' IS SEPARATED FROM B1 BY A THREE RESIDUE LOOP. HELIX A3 IS KINKED BY PRO A 91 AND HELIX B3 BY PRO B 91. |
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1dsb.cif.gz | 86.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1dsb.ent.gz | 66.6 KB | Display | PDB format |
PDBx/mmJSON format | 1dsb.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1dsb_validation.pdf.gz | 368.8 KB | Display | wwPDB validaton report |
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Full document | 1dsb_full_validation.pdf.gz | 371.1 KB | Display | |
Data in XML | 1dsb_validation.xml.gz | 8.5 KB | Display | |
Data in CIF | 1dsb_validation.cif.gz | 13.7 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ds/1dsb ftp://data.pdbj.org/pub/pdb/validation_reports/ds/1dsb | HTTPS FTP |
-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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Atom site foot note | 1: CIS PROLINE - PRO A 151 / 2: CIS PROLINE - PRO B 151 |
-Components
#1: Protein | Mass: 21155.025 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / References: UniProt: P24991, UniProt: P0AEG4*PLUS #2: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 2.78 Å3/Da / Density % sol: 55.78 % | ||||||||||||||||||||||||||||||||||||||||
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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
Radiation | Scattering type: x-ray |
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Radiation wavelength | Relative weight: 1 |
-Processing
Software |
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Refinement | Rfactor Rwork: 0.169 / Rfactor obs: 0.169 / Highest resolution: 2 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Highest resolution: 2 Å
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Refine LS restraints |
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Refinement | *PLUS Highest resolution: 2 Å / Lowest resolution: 6 Å / Num. reflection obs: 25426 / σ(I): 2 / Rfactor obs: 0.169 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS Type: x_angle_d / Dev ideal: 1.61 |