+Open data
-Basic information
Entry | Database: PDB / ID: 2frv | ||||||
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Title | CRYSTAL STRUCTURE OF THE OXIDIZED FORM OF NI-FE HYDROGENASE | ||||||
Components | (PERIPLASMIC HYDROGENASE) x 2 | ||||||
Keywords | OXIDOREDUCTASE / NI-FE HYDROGENASE | ||||||
Function / homology | Function and homology information cytochrome-c3 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 gigas (bacteria) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.54 Å | ||||||
Authors | Volbeda, A. / Frey, M. / Fontecilla-Camps, J.C. | ||||||
Citation | Journal: J.Am.Chem.Soc. / Year: 1996 Title: Structure of the [Nife] Hydrogenase Active Site: Evidence for Biologically Uncommon Fe Ligands Authors: Volbeda, A. / Garcin, E. / Piras, C. / De Lacey, A.L. / Fernandez, V.M. / Hatchikian, E.C. / Frey, M. / Fontecilla-Camps, J.C. #1: Journal: Nat.Struct.Biol. / Year: 1997 Title: Gas Access to the Active Site of Ni-Fe Hydrogenases Probed by X-Ray Crystallography and Molecular Dynamics Authors: Montet, Y. / Amara, P. / Volbeda, A. / Vernede, X. / Hatchikian, E.C. / Field, M.J. / Frey, M. / Fontecilla-Camps, J.C. #2: Journal: Nature / Year: 1995 Title: Crystal Structure of the Nickel-Iron Hydrogenase from Desulfovibrio Gigas Authors: Volbeda, A. / Charon, M.H. / Piras, C. / Hatchikian, E.C. / Frey, M. / Fontecilla-Camps, J.C. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2frv.cif.gz | 904.6 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2frv.ent.gz | 741.6 KB | Display | PDB format |
PDBx/mmJSON format | 2frv.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/fr/2frv ftp://data.pdbj.org/pub/pdb/validation_reports/fr/2frv | HTTPS FTP |
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-Related structure data
Related structure data | 1frvS S: Starting model for refinement |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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2 |
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3 |
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4 |
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5 |
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6 |
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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS oper:
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Details | THERE ARE SIX MOLECULES PER (TRICLINIC) UNIT CELL. EACH OF THESE CONSISTS OF ONE SMALL AND ONE LARGE SUBUNIT. IN ALL STAGES THE SIX HYDROGENASE MOLECULES WERE CONSTRAINED TO OBEY EXACT NON-CRYSTALLOGRAPHIC SYMMETRY. |
-Components
-Protein , 2 types, 12 molecules SACEGILBDFHJ
#1: Protein | Mass: 28351.396 Da / Num. of mol.: 6 / Source method: isolated from a natural source / Source: (natural) Desulfovibrio gigas (bacteria) / Cellular location: PERIPLASM / References: UniProt: P12943, 1.18.99.1 #2: Protein | Mass: 59571.938 Da / Num. of mol.: 6 / Source method: isolated from a natural source / Source: (natural) Desulfovibrio gigas (bacteria) / Cellular location: PERIPLASM / References: UniProt: P12944, 1.18.99.1 |
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-Non-polymers , 7 types, 1188 molecules
#3: Chemical | ChemComp-SF4 / #4: Chemical | ChemComp-F3S / #5: Chemical | ChemComp-NI / #6: Chemical | ChemComp-MG / #7: Chemical | ChemComp-FCO / #8: Chemical | ChemComp-O / #9: Water | ChemComp-HOH / | |
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-Details
Nonpolymer details | THE ACTIVE SITE CONTAINS TWO METALS: NI AND FE. THE LATTER ASSIGNMENT HAS BEEN CONFIRMED BY ...THE ACTIVE SITE CONTAINS TWO METALS: NI AND FE. THE LATTER ASSIGNMENT |
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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: 2.8 Å3/Da / Density % sol: 56.14 % |
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Crystal grow | pH: 6.6 / Details: pH 6.6 |
Crystal grow | *PLUS Method: unknown |
-Data collection
Diffraction | Mean temperature: 120 K |
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Diffraction source | Source: SYNCHROTRON / Site: ESRF / Beamline: ID2 / Wavelength: 0.905 |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Jun 1, 1994 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.905 Å / Relative weight: 1 |
Reflection | Resolution: 2.54→29.36 Å / Num. obs: 174383 / % possible obs: 92.5 % / Observed criterion σ(I): 4 / Redundancy: 1.7 % / Biso Wilson estimate: 7.3 Å2 / Rmerge(I) obs: 0.066 / Net I/σ(I): 7.5 |
Reflection shell | Resolution: 2.54→2.84 Å / Redundancy: 1.57 % / Rmerge(I) obs: 0.151 / Mean I/σ(I) obs: 4 / % possible all: 87.4 |
Reflection | *PLUS Num. measured all: 296283 |
Reflection shell | *PLUS % possible obs: 87.4 % |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 1FRV, MOLECULE 1 Resolution: 2.54→8 Å / Cross valid method: R-FREE / σ(F): 0 / Details: BEFORE PROLSQ: AMORE + X-PLOR
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Displacement parameters | Biso mean: 9.2 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine analyze | Luzzati d res low obs: 20 Å / Luzzati sigma a obs: 0.27 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.54→8 Å
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Refine LS restraints |
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