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- PDB-2qfg: Solution Structure of the N-terminal SCR-1/5 fragment of Compleme... -
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Open data
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Basic information
Entry | Database: PDB / ID: 2qfg | ||||||
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Title | Solution Structure of the N-terminal SCR-1/5 fragment of Complement Factor H. | ||||||
![]() | Complement factor H | ||||||
![]() | IMMUNE SYSTEM / X-ray scattering / complement / SCR domain / Factor H / Age-related macular degeneration / Complement alternate pathway / Disease mutation / Glycoprotein / Immune response / Innate immunity / Sushi | ||||||
Function / homology | ![]() regulation of complement activation, alternative pathway / symbiont cell surface / complement component C3b binding / regulation of complement-dependent cytotoxicity / regulation of complement activation / heparan sulfate proteoglycan binding / serine-type endopeptidase complex / complement activation, alternative pathway / complement activation / Regulation of Complement cascade ...regulation of complement activation, alternative pathway / symbiont cell surface / complement component C3b binding / regulation of complement-dependent cytotoxicity / regulation of complement activation / heparan sulfate proteoglycan binding / serine-type endopeptidase complex / complement activation, alternative pathway / complement activation / Regulation of Complement cascade / heparin binding / blood microparticle / proteolysis / extracellular space / extracellular exosome / extracellular region / identical protein binding Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() | ||||||
![]() | Okemefuna, A.I. / Gilbert, H.E. / Griggs, K.M. / Ormsby, R.J. / Gordon, D.L. / Perkins, S.J. | ||||||
![]() | ![]() Title: The regulatory SCR-1/5 and cell surface-binding SCR-16/20 fragments of factor H reveal partially folded-back solution structures and different self-associative properties. Authors: Okemefuna, A.I. / Gilbert, H.E. / Griggs, K.M. / Ormsby, R.J. / Gordon, D.L. / Perkins, S.J. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 86.9 KB | Display | ![]() |
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PDB format | ![]() | 57.5 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 320.5 KB | Display | ![]() |
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Full document | ![]() | 324.5 KB | Display | |
Data in XML | ![]() | 2.1 KB | Display | |
Data in CIF | ![]() | 23.8 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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Links
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Assembly
Deposited unit | ![]()
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1 |
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Number of models | 9 |
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Components
#1: Protein | Mass: 35434.668 Da / Num. of mol.: 1 / Fragment: SCR domains 1-5 (residues 19-322) Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Description: Protein was purified by Nickel affinity and size exclusion chromatography. Gene: CFH, HF, HF1, HF2 / Production host: ![]() |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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-Data collection
Detector | Date: May 24, 2006 |
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Radiation | Monochromator: MIRROR / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Relative weight: 1 |
Soln scatter | Type: x-ray Buffer name: 137 MM NACL 2.5 MM KCL 8.1 MM NA2HPO4 1.5 MM KH2PO4 Conc. range: 0.21-0.84 / Data analysis software list: SCTPL7, GNOM / Data reduction software list: MULTICCD / Detector type: FRELON CCD CAMERA / Mean guiner radius: 4.26 nm / Mean guiner radius esd: 0.16 nm / Min mean cross sectional radii gyration: 1.46 nm / Min mean cross sectional radii gyration esd: 0.08 nm / Num. of time frames: 10 / Protein length: 1 / Sample pH: 7.3 / Source beamline: IDO2 / Source class: Y / Source type: ESRF GRENOBLE / Temperature: 296 K |
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Processing
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Refinement step | Cycle: LAST
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Soln scatter model | Details: TWELVE SOLUTION STRUCTURES ARE DEPOSITED. THE FIRST OF THESE CORRESPONDS TO THE BEST-FIT STRUCTURE IN THE PRIMARY CITATION, WHILE THE OTHER ELEVEN CORRESPOND TO THOSE ADDITIONALLY SHOWN IN ...Details: TWELVE SOLUTION STRUCTURES ARE DEPOSITED. THE FIRST OF THESE CORRESPONDS TO THE BEST-FIT STRUCTURE IN THE PRIMARY CITATION, WHILE THE OTHER ELEVEN CORRESPOND TO THOSE ADDITIONALLY SHOWN IN FIGURE 11(A) OF THE PRIMARY CITATION Num. of conformers submitted: 12 / Representative conformer: 1 / Software list: INSIGHT II, SCTPL7, GNOM |