+Open data
-Basic information
Entry | Database: PDB / ID: 4c1n | ||||||
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Title | Corrinoid protein reactivation complex with activator | ||||||
Components |
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Keywords | OXIDOREDUCTASE/METAL BINDING PROTEIN / OXIDOREDUCTASE-METAL BINDING PROTEIN COMPLEX | ||||||
Function / homology | Function and homology information acetyl-CoA catabolic process / methyltransferase activity / 2 iron, 2 sulfur cluster binding / 4 iron, 4 sulfur cluster binding / iron ion binding / metal ion binding Similarity search - Function | ||||||
Biological species | CARBOXYDOTHERMUS HYDROGENOFORMANS (bacteria) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / OTHER / Resolution: 2.53 Å | ||||||
Authors | Hennig, S.E. / Goetzl, S. / Jeoung, J.H. / Bommer, M. / Lendzian, F. / Hildebrandt, P. / Dobbek, H. | ||||||
Citation | Journal: Nat.Commun. / Year: 2014 Title: ATP-Induced Electron Transfer by Redox-Selective Partner Recognition Authors: Hennig, S.E. / Goetzl, S. / Jeoung, J.H. / Bommer, M. / Lendzian, F. / Hildebrandt, P. / Dobbek, H. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 4c1n.cif.gz | 975.8 KB | Display | PDBx/mmCIF format |
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PDB format | pdb4c1n.ent.gz | 799.9 KB | Display | PDB format |
PDBx/mmJSON format | 4c1n.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 4c1n_validation.pdf.gz | 1.6 MB | Display | wwPDB validaton report |
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Full document | 4c1n_full_validation.pdf.gz | 1.7 MB | Display | |
Data in XML | 4c1n_validation.xml.gz | 178.2 KB | Display | |
Data in CIF | 4c1n_validation.cif.gz | 244.3 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/c1/4c1n ftp://data.pdbj.org/pub/pdb/validation_reports/c1/4c1n | HTTPS FTP |
-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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2 |
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3 |
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4 |
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Unit cell |
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-Components
-Protein , 2 types, 8 molecules ACEGBDFH
#1: Protein | Mass: 48125.395 Da / Num. of mol.: 4 / Fragment: RESIDUES 2-443 Source method: isolated from a genetically manipulated source Source: (gene. exp.) CARBOXYDOTHERMUS HYDROGENOFORMANS (bacteria) Production host: ESCHERICHIA COLI (E. coli) / References: UniProt: Q3ACS3 #2: Protein | Mass: 33779.160 Da / Num. of mol.: 4 / Fragment: RESIDUES 2-310 Source method: isolated from a genetically manipulated source Source: (gene. exp.) CARBOXYDOTHERMUS HYDROGENOFORMANS (bacteria) Production host: ESCHERICHIA COLI (E. coli) / References: UniProt: Q3ACS0 |
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-IRON-SULFUR CLUSTER BINDING ... , 2 types, 4 molecules IJXK
#3: Protein | Mass: 55291.496 Da / Num. of mol.: 3 / Fragment: RESIDUES 122-630 Source method: isolated from a genetically manipulated source Source: (gene. exp.) CARBOXYDOTHERMUS HYDROGENOFORMANS (bacteria) Production host: ESCHERICHIA COLI (E. coli) / References: UniProt: Q3ACS2 #4: Protein | | Mass: 55420.609 Da / Num. of mol.: 1 / Fragment: RESIDUES 121-630 Source method: isolated from a genetically manipulated source Source: (gene. exp.) CARBOXYDOTHERMUS HYDROGENOFORMANS (bacteria) Production host: ESCHERICHIA COLI (E. coli) / References: UniProt: Q3ACS2 |
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-Non-polymers , 3 types, 1206 molecules
#5: Chemical | ChemComp-SF4 / #6: Chemical | ChemComp-B12 / #7: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 2.48 Å3/Da / Density % sol: 50.37 % / Description: NONE |
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: BESSY / Beamline: 14.2 / Wavelength: 0.9184 |
Detector | Type: MARMOSAIC 225 mm CCD / Detector: CCD / Date: Dec 15, 2011 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9184 Å / Relative weight: 1 |
Reflection | Resolution: 2.53→30 Å / Num. obs: 168978 / % possible obs: 96 % / Observed criterion σ(I): 2.6 / Redundancy: 2.74 % / Rmerge(I) obs: 0.09 / Net I/σ(I): 10 |
Reflection shell | Resolution: 2.53→2.6 Å / Redundancy: 2.7 % / Rmerge(I) obs: 0.54 / Mean I/σ(I) obs: 2.6 / % possible all: 85 |
-Processing
Software |
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Refinement | Method to determine structure: OTHER Starting model: NONE Resolution: 2.53→30.631 Å / SU ML: 0.33 / σ(F): 1.99 / Phase error: 24.72 / Stereochemistry target values: ML
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.53→30.631 Å
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Refine LS restraints |
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LS refinement shell |
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