+Open data
-Basic information
Entry | Database: PDB / ID: 1i0s | ||||||
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Title | ARCHAEOGLOBUS FULGIDUS FERRIC REDUCTASE COMPLEX WITH NADP+ | ||||||
Components | CONSERVED HYPOTHETICAL PROTEIN | ||||||
Keywords | OXIDOREDUCTASE / six stranded antiparallel beta-barrel / FMN and NADP+ binding domain | ||||||
Function / homology | Function and homology information ferric-chelate reductase [NAD(P)H] / ferric-chelate reductase (NADH) activity / oxidoreductase activity, acting on metal ions, NAD or NADP as acceptor / ferric-chelate reductase (NADPH) activity / pyrimidine nucleobase catabolic process / riboflavin reductase (NADPH) activity / FMN binding / protein homodimerization activity Similarity search - Function | ||||||
Biological species | Archaeoglobus fulgidus (archaea) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.65 Å | ||||||
Authors | Chiu, H.-J. / Johnson, E. / Schroder, I. / Rees, D.C. | ||||||
Citation | Journal: Structure / Year: 2001 Title: Crystal structures of a novel ferric reductase from the hyperthermophilic archaeon Archaeoglobus fulgidus and its complex with NADP+. Authors: Chiu, H.J. / Johnson, E. / Schroder, I. / Rees, D.C. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1i0s.cif.gz | 85 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1i0s.ent.gz | 63 KB | Display | PDB format |
PDBx/mmJSON format | 1i0s.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1i0s_validation.pdf.gz | 545.8 KB | Display | wwPDB validaton report |
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Full document | 1i0s_full_validation.pdf.gz | 550.5 KB | Display | |
Data in XML | 1i0s_validation.xml.gz | 9.3 KB | Display | |
Data in CIF | 1i0s_validation.cif.gz | 14.5 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/i0/1i0s ftp://data.pdbj.org/pub/pdb/validation_reports/i0/1i0s | HTTPS FTP |
-Related structure data
Related structure data | 1i0rSC 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: 18683.279 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Archaeoglobus fulgidus (archaea) / Strain: AF0830 / Production host: Escherichia coli (E. coli) / References: UniProt: O29428 #2: Chemical | ChemComp-FMN / | #3: Chemical | ChemComp-NAP / | #4: 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: 2.43 Å3/Da / Density % sol: 49 % | ||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 277 K / Method: vapor diffusion, hanging drop / pH: 8.4 Details: PEG4000, SODIUM ACETATE, TRIS-HCL, pH 8.4, VAPOR DIFFUSION, HANGING DROP, temperature 277K | ||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 4 ℃ / pH: 7.5 | ||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: SSRL / Beamline: BL9-1 / Wavelength: 0.98 Å |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Sep 20, 1999 / Details: MIRRORS |
Radiation | Monochromator: CYCLINDRICALLY BENT CUBED ROOT SI(311) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.98 Å / Relative weight: 1 |
Reflection | Resolution: 1.65→20 Å / Num. all: 36289 / Num. obs: 35546 / % possible obs: 0.846 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 4.6 % / Biso Wilson estimate: 15.8 Å2 / Rmerge(I) obs: 0.054 / Net I/σ(I): 15.6 |
Reflection shell | Resolution: 1.65→1.71 Å / Redundancy: 4.5 % / Rmerge(I) obs: 0.204 / % possible all: 86.5 |
Reflection | *PLUS % possible obs: 86.1 % / Num. measured all: 168005 |
Reflection shell | *PLUS % possible obs: 86.5 % |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 1I0R Resolution: 1.65→20 Å / Data cutoff high rms absF: 0 / Isotropic thermal model: ISOTROPIC / Cross valid method: THROUGHOUT / σ(F): 0 / σ(I): 0 / Stereochemistry target values: ENGH & HUBER
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Displacement parameters | Biso mean: 19.98 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 1.65→20 Å
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Refine LS restraints |
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Xplor file | Serial no: 1 / Param file: FMN.PAR / Topol file: FMN.TOP | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Software | *PLUS Name: CNS / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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