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Yorodumi- PDB-6rtp: THE 3D STRUCTURE OF [NIFESE] HYDROGENASE G50T VaRIANT FROM DESULF... -
+Open data
-Basic information
Entry | Database: PDB / ID: 6rtp | |||||||||
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Title | THE 3D STRUCTURE OF [NIFESE] HYDROGENASE G50T VaRIANT FROM DESULFOVIBRIO VULGARIS HILDENBOROUGH AT 1.10 ANGSTROM RESOLUTION | |||||||||
Components | (Periplasmic [NiFeSe] hydrogenase, ...) x 2 | |||||||||
Keywords | OXIDOREDUCTASE / NIFESE-SITE / H2 CLEAVAGE/PRODUCTION / O2 TOLERANCE | |||||||||
Function / homology | Function and homology information cytochrome-c3 hydrogenase / ferredoxin hydrogenase / cytochrome-c3 hydrogenase activity / ferredoxin hydrogenase complex / ferredoxin hydrogenase activity / 3 iron, 4 sulfur cluster binding / nickel cation binding / 4 iron, 4 sulfur cluster binding / periplasmic space / metal ion binding Similarity search - Function | |||||||||
Biological species | Desulfovibrio vulgaris (bacteria) | |||||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / molecular replacement / Resolution: 1.1 Å | |||||||||
Authors | Matias, P.M. / Zacarias, S. / Pereita, I. | |||||||||
Funding support | Portugal, 2items
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Citation | Journal: Acs Catalysis / Year: 2019 Title: A Hydrophilic Channel Is Involved in Oxidative Inactivation of a [NiFeSe] Hydrogenase Authors: Zacarias, S. / Temporao, A. / del Barrio, M. / Fourmond, V. / Leger, C. / Matias, P.M. / Pereira, I.A.C. | |||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 6rtp.cif.gz | 562.2 KB | Display | PDBx/mmCIF format |
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PDB format | pdb6rtp.ent.gz | 382.5 KB | Display | PDB format |
PDBx/mmJSON format | 6rtp.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/rt/6rtp ftp://data.pdbj.org/pub/pdb/validation_reports/rt/6rtp | HTTPS FTP |
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-Related structure data
Related structure data | 6ru9C 6rucC 5jshS 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
-Periplasmic [NiFeSe] hydrogenase, ... , 2 types, 2 molecules AB
#1: Protein | Mass: 30261.568 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Desulfovibrio vulgaris (strain Hildenborough / ATCC 29579 / DSM 644 / NCIMB 8303) (bacteria) Gene: hysB, DVU_1917 Production host: Desulfovibrio vulgaris str. Hildenborough (bacteria) References: UniProt: Q72AS4, ferredoxin hydrogenase |
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#2: Protein | Mass: 54469.246 Da / Num. of mol.: 1 / Mutation: G50T Source method: isolated from a genetically manipulated source Details: Cys 75 partially oxidized to sulfenate/sulfinate Source: (gene. exp.) Desulfovibrio vulgaris (strain Hildenborough / ATCC 29579 / DSM 644 / NCIMB 8303) (bacteria) Gene: hysA, DVU_1918 Production host: Desulfovibrio vulgaris str. Hildenborough (bacteria) References: UniProt: Q72AS3, ferredoxin hydrogenase |
-Non-polymers , 9 types, 811 molecules
#3: Chemical | #4: Chemical | ChemComp-6ML / | #5: Chemical | #6: Chemical | ChemComp-FCO / | #7: Chemical | ChemComp-NI / | #8: Chemical | ChemComp-FE2 / | #9: Chemical | ChemComp-H2S / | #10: Chemical | ChemComp-CL / | #11: 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: 2.12 Å3/Da / Density % sol: 41.93 % / Description: Plate |
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Crystal grow | Temperature: 295 K / Method: vapor diffusion, sitting drop / pH: 7 / Details: 20% PEG 1500 (w/v), 0.1 M Tris-HCl pH 7 |
-Data collection
Diffraction | Mean temperature: 100 K / Serial crystal experiment: N | ||||||||||||||||||||||||||||||
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Diffraction source | Source: SYNCHROTRON / Site: ESRF / Beamline: ID29 / Wavelength: 0.8856 Å | ||||||||||||||||||||||||||||||
Detector | Type: DECTRIS PILATUS3 6M / Detector: PIXEL / Date: Dec 13, 2014 | ||||||||||||||||||||||||||||||
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray | ||||||||||||||||||||||||||||||
Radiation wavelength | Wavelength: 0.8856 Å / Relative weight: 1 | ||||||||||||||||||||||||||||||
Reflection | Resolution: 1.1→45.38 Å / Num. obs: 263501 / % possible obs: 93.3 % / Redundancy: 2.3 % / Biso Wilson estimate: 11.03 Å2 / CC1/2: 0.994 / Rmerge(I) obs: 0.076 / Rpim(I) all: 0.061 / Rrim(I) all: 0.098 / Net I/σ(I): 6.1 / Num. measured all: 617436 | ||||||||||||||||||||||||||||||
Reflection shell | Diffraction-ID: 1
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-Phasing
Phasing | Method: molecular replacement | |||||||||
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Phasing MR | Model details: Phaser MODE: MR_AUTO
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-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 5JSH Resolution: 1.1→45.38 Å / SU ML: 0.1206 / Cross valid method: THROUGHOUT / σ(F): 0.01 / Phase error: 18.2096 Stereochemistry target values: GeoStd + Monomer Library + CDL v1.2
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 15.24 Å2 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.1→45.38 Å
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Refine LS restraints |
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LS refinement shell |
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