+Open data
-Basic information
Entry | Database: PDB / ID: 2bhf | ||||||
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Title | 3D structure of the reduced form of CotA | ||||||
Components | SPORE COAT PROTEIN A | ||||||
Keywords | OXIDOREDUCTASE / MULTICOPPER-OXIDASE / LACCASE / OXYGEN REDUCTION | ||||||
Function / homology | Function and homology information bilirubin oxidase / laccase / sporulation resulting in formation of a cellular spore / outer membrane-bounded periplasmic space / oxidoreductase activity / copper ion binding Similarity search - Function | ||||||
Biological species | BACILLUS SUBTILIS (bacteria) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.5 Å | ||||||
Authors | Bento, I. / Martins, L.O. / Lopes, G.G. / Carrondo, M.A. / Lindley, P.F. | ||||||
Citation | Journal: Dalton Trans. / Year: 2005 Title: Dioxygen Reduction by Multi-Copper Oxidases; a Structural Perspective. Authors: Bento, I. / Martins, L.O. / Lopes, G.G. / Carrondo, M.A. / Lindley, P.F. | ||||||
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. |
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2bhf.cif.gz | 120 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2bhf.ent.gz | 92.4 KB | Display | PDB format |
PDBx/mmJSON format | 2bhf.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2bhf_validation.pdf.gz | 414.1 KB | Display | wwPDB validaton report |
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Full document | 2bhf_full_validation.pdf.gz | 318.2 KB | Display | |
Data in XML | 2bhf_validation.xml.gz | 18.8 KB | Display | |
Data in CIF | 2bhf_validation.cif.gz | 29.7 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/bh/2bhf ftp://data.pdbj.org/pub/pdb/validation_reports/bh/2bhf | HTTPS FTP |
-Related structure data
Related structure data | 1w6lC 1w6wC 1w8eC 1gskS 1hkp 1hkz 1hl0 1hl1 1ogr S: Starting model for refinement C: citing same article (ref.) |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 58574.789 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) BACILLUS SUBTILIS (bacteria) / Production host: ESCHERICHIA COLI (E. coli) / References: UniProt: P07788 | ||||
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#2: Chemical | ChemComp-CU1 / #3: Chemical | #4: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 3.35 Å3/Da / Density % sol: 62.95 % |
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-Data collection
Diffraction | Mean temperature: 110 K |
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Diffraction source | Source: SYNCHROTRON / Site: ESRF / Beamline: ID14-1 / Wavelength: 0.934 |
Detector | Type: ADSC CCD / Detector: CCD |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.934 Å / Relative weight: 1 |
Reflection | Resolution: 2.5→30 Å / Num. obs: 28950 / % possible obs: 99.5 % / Observed criterion σ(I): 2 / Redundancy: 3.63 % / Rmerge(I) obs: 0.04 / Net I/σ(I): 28.2 |
Reflection shell | Resolution: 2.5→2.59 Å / Redundancy: 3.69 % / Rmerge(I) obs: 0.31 / Mean I/σ(I) obs: 3.44 / % possible all: 98.9 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 1GSK Resolution: 2.5→29.49 Å / Cor.coef. Fo:Fc: 0.96 / Cor.coef. Fo:Fc free: 0.941 / SU B: 6.564 / SU ML: 0.145 / Cross valid method: THROUGHOUT / ESU R: 0.293 / ESU R Free: 0.217 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 45.18 Å2
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Refinement step | Cycle: LAST / Resolution: 2.5→29.49 Å
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Refine LS restraints |
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