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Yorodumi- PDB-2ic4: Solution structure of the His402 allotype of the Factor H SCR6-SC... -
+Open data
-Basic information
Entry | Database: PDB / ID: 2ic4 | ||||||
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Title | Solution structure of the His402 allotype of the Factor H SCR6-SCR7-SCR8 fragment | ||||||
Components | Complement factor HFactor H | ||||||
Keywords | IMMUNE SYSTEM / Factor H / X-ray scattering / homology modelling / ultracentrifugation | ||||||
Function / homology | Function and homology information 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 | Homo sapiens (human) | ||||||
Method | SOLUTION SCATTERING / SYNCHROTRON | ||||||
Model type details | CA ATOMS ONLY | ||||||
Authors | Fernando, A.N. / Furtado, P.B. / Gilbert, H.E. / Clark, S.J. / Day, A.J. / Sim, R.B. / Perkins, S.J. | ||||||
Citation | Journal: J.Mol.Biol. / Year: 2007 Title: Associative and Structural Properties of the Region of Complement Factor H Encompassing the Tyr402His Disease-related Polymorphism and its Interactions with Heparin. Authors: Fernando, A.N. / Furtado, P.B. / Clark, S.J. / Gilbert, H.E. / Day, A.J. / Sim, R.B. / Perkins, S.J. #1: Journal: J.Mol.Biol. / Year: 2001 Title: Folded-back Solution Structure of Monomeric Factor H of Human Complement by Synchrotron X-ray and Neutron Scattering, Analytical Ultracentrifugation and Constrained Molecular Modelling Authors: Aslam, M. / Perkins, S.J. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2ic4.cif.gz | 17.4 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2ic4.ent.gz | 7.2 KB | Display | PDB format |
PDBx/mmJSON format | 2ic4.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ic/2ic4 ftp://data.pdbj.org/pub/pdb/validation_reports/ic/2ic4 | HTTPS FTP |
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-Related structure data
Related structure data | |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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-Components
#1: Protein | Mass: 21141.785 Da / Num. of mol.: 1 / Fragment: Factor H SCR6-SCR7-SCR8 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: CFH, HF, HF1 / Plasmid: pET14b / Species (production host): Escherichia coli / Production host: Escherichia coli BL21 (bacteria) / Strain (production host): BL21 / References: UniProt: P08603 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION SCATTERING |
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-Sample preparation
Crystal grow | Temperature: 288 K / pH: 7.3 / Details: SOLUTION, pH 7.3, temperature 288K |
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-Data collection
Diffraction |
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Diffraction source | Source: SYNCHROTRON / Site: ESRF / Beamline: ID09 / Wavelength: 1 Å | |||||||||
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray | |||||||||
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 | |||||||||
Soln scatter | Type: x-ray Buffer name: 9.6 MM NA, K PHOSPHATE 137 MM NACL 3 MM KCL 8 MM NA2HPO4 1 MM KH2PO4 Conc. range: 0.38-0.55 / Data analysis software list: SCTPL7, GNOM / Data reduction software list: MULTICCD / Detector type: FRELON CCD CAMERA / Mean guiner radius: 3.12 nm / Mean guiner radius esd: 0.16 nm / Min mean cross sectional radii gyration: 1.04 nm / Min mean cross sectional radii gyration esd: 0.06 nm / Num. of time frames: 10 / Protein length: 0.5 / Sample pH: 7.3 / Source beamline: IDO2 / Source class: Y / Source type: ESRF GRENOBLE / Temperature: 288 K |
-Processing
Software |
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Refinement step | Cycle: LAST
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Soln scatter model | Details: THE INFORMATION FOR THE HIS402 ALLOTYPE IS LISTED FIRST IN REMARK 265. THE INFORMATION FOR THE TYR402 ALLOTYPE IS LISTED SECOND. THE COORDINATES CONTAIN ONLY CA ATOMS. THE SECOND SET OF ...Details: THE INFORMATION FOR THE HIS402 ALLOTYPE IS LISTED FIRST IN REMARK 265. THE INFORMATION FOR THE TYR402 ALLOTYPE IS LISTED SECOND. THE COORDINATES CONTAIN ONLY CA ATOMS. THE SECOND SET OF RADII: MEAN RADIUS OF GYRATION IS 3.26 NM WITH SIGMA MEAN 0.20. R MEAN CROSS SECTIONAL RADII IS 1.15 NM WITH SIGMA MEAN 0.13. Num. of conformers submitted: 1 / Software list: INSIGHT II, SCTPL7, GNOM |