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Yorodumi- PDB-5odq: Heterodisulfide reductase / [NiFe]-hydrogenase complex from Metha... -
+Open data
-Basic information
Entry | Database: PDB / ID: 5odq | ||||||
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Title | Heterodisulfide reductase / [NiFe]-hydrogenase complex from Methanothermococcus thermolithotrophicus soaked with bromoethanesulfonate. | ||||||
Components |
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Keywords | OXIDOREDUCTASE / Heterodisulfide reductase / [NiFe]-hydrogenase / FeS cluster / ferredoxin / CCG motif / methanogenesis / flavoprotein / flavin-based electron bifurcation / [2Fe-2S] cluster / macromolecular complex / anaerobic / thioredoxin / bromoethanesulfonate / metabolism | ||||||
Function / homology | Function and homology information dihydromethanophenazine:CoB-CoM heterodisulfide reductase / hydrogen dehydrogenase / hydrogen dehydrogenase activity / CoB--CoM heterodisulfide reductase activity / Oxidoreductases; Acting on a sulfur group of donors / hydrogenase (acceptor) / methanogenesis / hydrogenase (acceptor) activity / ferredoxin hydrogenase activity / iron-sulfur cluster binding ...dihydromethanophenazine:CoB-CoM heterodisulfide reductase / hydrogen dehydrogenase / hydrogen dehydrogenase activity / CoB--CoM heterodisulfide reductase activity / Oxidoreductases; Acting on a sulfur group of donors / hydrogenase (acceptor) / methanogenesis / hydrogenase (acceptor) activity / ferredoxin hydrogenase activity / iron-sulfur cluster binding / nickel cation binding / 2 iron, 2 sulfur cluster binding / 4 iron, 4 sulfur cluster binding / oxidoreductase activity / metal ion binding Similarity search - Function | ||||||
Biological species | Methanothermococcus thermolithotrophicus DSM 2095 (archaea) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.15 Å | ||||||
Authors | Wagner, T. / Koch, J. / Ermler, U. / Shima, S. | ||||||
Citation | Journal: Science / Year: 2017 Title: Methanogenic heterodisulfide reductase (HdrABC-MvhAGD) uses two noncubane [4Fe-4S] clusters for reduction. Authors: Wagner, T. / Koch, J. / Ermler, U. / Shima, S. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 5odq.cif.gz | 1.5 MB | Display | PDBx/mmCIF format |
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PDB format | pdb5odq.ent.gz | 1.3 MB | Display | PDB format |
PDBx/mmJSON format | 5odq.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/od/5odq ftp://data.pdbj.org/pub/pdb/validation_reports/od/5odq | HTTPS FTP |
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-Related structure data
Related structure data | 5odcSC 5odhC 5odiC 5odrC 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
-Heterodisulfide reductase, subunit ... , 3 types, 6 molecules AGBHCI
#1: Protein | Mass: 71591.672 Da / Num. of mol.: 2 / Mutation: Wild-type / Source method: isolated from a natural source Source: (natural) Methanothermococcus thermolithotrophicus DSM 2095 (archaea) Cell line: / / Organ: / / Variant: / / Tissue: / References: UniProt: A0A2D0TCB9*PLUS, dihydromethanophenazine:CoB-CoM heterodisulfide reductase #2: Protein | Mass: 32075.318 Da / Num. of mol.: 2 / Mutation: Wild-type / Source method: isolated from a natural source Details: This subunit contains two pentacoordinated non cubane [4Fe-4S] cluster Source: (natural) Methanothermococcus thermolithotrophicus DSM 2095 (archaea) Cell line: / / Organ: / / Variant: / / Tissue: / References: UniProt: A0A2D0TCB4*PLUS, dihydromethanophenazine:CoB-CoM heterodisulfide reductase #3: Protein | Mass: 20483.650 Da / Num. of mol.: 2 / Mutation: Wild-type / Source method: isolated from a natural source Source: (natural) Methanothermococcus thermolithotrophicus DSM 2095 (archaea) Cell line: / / Organ: / / Variant: / / Tissue: / References: UniProt: A0A2D0TC97*PLUS, dihydromethanophenazine:CoB-CoM heterodisulfide reductase |
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-Methyl-viologen reducing hydrogenase, subunit ... , 3 types, 6 molecules DJEKFL
#4: Protein | Mass: 16057.495 Da / Num. of mol.: 2 / Mutation: Wild-type / Source method: isolated from a natural source Source: (natural) Methanothermococcus thermolithotrophicus DSM 2095 (archaea) Cell line: / / Organ: / / Variant: / / Tissue: / References: UniProt: A0A2D0TC98*PLUS, dihydromethanophenazine:CoB-CoM heterodisulfide reductase #5: Protein | Mass: 32511.432 Da / Num. of mol.: 2 / Mutation: Wild-type / Source method: isolated from a natural source Source: (natural) Methanothermococcus thermolithotrophicus DSM 2095 (archaea) Cell line: / / Organ: / / Variant: / / Tissue: / References: UniProt: A0A2D0TC99*PLUS, hydrogenase (acceptor) #6: Protein | Mass: 53129.602 Da / Num. of mol.: 2 / Mutation: Wild-type / Source method: isolated from a natural source Details: The C-terminus has been post-translationally cleaved Source: (natural) Methanothermococcus thermolithotrophicus DSM 2095 (archaea) Cell line: / / Organ: / / Variant: / / Tissue: / References: UniProt: A0A2D0TCA6*PLUS, hydrogenase (acceptor) |
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-Non-polymers , 12 types, 970 molecules
#7: Chemical | #8: Chemical | ChemComp-ACT / #9: Chemical | ChemComp-SF4 / #10: Chemical | ChemComp-GOL / #11: Chemical | ChemComp-9S8 / #12: Chemical | ChemComp-9SB / #13: Chemical | #14: Chemical | ChemComp-TRS / | #15: Chemical | #16: Chemical | #17: Chemical | #18: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.17 Å3/Da / Density % sol: 43.36 % Description: Black thick plate square shape of about 0.2-0.4 mm length. |
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Crystal grow | Temperature: 294 K / Method: vapor diffusion, sitting drop / pH: 8.5 Details: All crystallization was performed in an anaerobic chamber (95% N2/5% H2) with anoxic solution using the sitting drop method (96-well 2-drop MRC Crystallization Plates in polystyrene, ...Details: All crystallization was performed in an anaerobic chamber (95% N2/5% H2) with anoxic solution using the sitting drop method (96-well 2-drop MRC Crystallization Plates in polystyrene, Molecular Dimensions, Suffolk, UK). The crystallization reservoir contained 100 mM Tris/HCl, pH 8.5, 30% (w/v) polyethylene glycol 4000, and 200 mM Na acetate trihydrate. Crystallization drop contained 1 ul HdrABC-MvhAGD at 25 mg/ml premixed with 2 mM FAD and 1 ul of precipitant. The soaking experiment with the bromoethanesulfonate was done by soaking the crystals in the same crystallization solution supplemented with 66 mM of bromoethanesulfonate for 7 min. The crystal has been cryo-protected using the the mother liquor solution supplemented with 30% glycerol and 10 mM bromoethanesulfonate. |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: SLS / Beamline: X10SA / Wavelength: 0.91941 Å |
Detector | Type: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Jun 23, 2016 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.91941 Å / Relative weight: 1 |
Reflection | Resolution: 2.15→48.85 Å / Num. obs: 241487 / % possible obs: 100 % / Redundancy: 6.9 % / Biso Wilson estimate: 17.13 Å2 / CC1/2: 0.991 / Rmerge(I) obs: 0.21 / Rpim(I) all: 0.086 / Net I/σ(I): 8 |
Reflection shell | Resolution: 2.15→2.27 Å / Redundancy: 6.8 % / Rmerge(I) obs: 0.606 / Mean I/σ(I) obs: 3.3 / Num. unique obs: 35106 / CC1/2: 0.327 / Rpim(I) all: 0.249 / % possible all: 100 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 5ODC Resolution: 2.15→48.68 Å / Cor.coef. Fo:Fc: 0.9051 / Cor.coef. Fo:Fc free: 0.8848 / Cross valid method: THROUGHOUT / σ(F): 0 / SU R Blow DPI: 0.217 / SU Rfree Blow DPI: 0.167
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Displacement parameters | Biso mean: 33.25 Å2
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Refine analyze | Luzzati coordinate error obs: 0.291 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: 1 / Resolution: 2.15→48.68 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.15→2.21 Å / Total num. of bins used: 20
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Refinement TLS params. | Method: refined / Refine-ID: X-RAY DIFFRACTION
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Refinement TLS group |
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