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- PDB-2xqw: Structure of Factor H domains 19-20 in complex with complement C3d -
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Open data
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Basic information
Entry | Database: PDB / ID: 2xqw | ||||||
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Title | Structure of Factor H domains 19-20 in complex with complement C3d | ||||||
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![]() | IMMUNE SYSTEM / COMPLEMENT ALTERNATIVE PATHWAY / ATYPICAL HEMOLYTIC UREMIC SYNDROME / AHUS / CFH / FH / C3B | ||||||
Function / homology | ![]() regulation of complement activation, alternative pathway / symbiont cell surface / oviduct epithelium development / C5L2 anaphylatoxin chemotactic receptor binding / regulation of triglyceride biosynthetic process / positive regulation of activation of membrane attack complex / complement component C3b binding / regulation of complement-dependent cytotoxicity / vertebrate eye-specific patterning / positive regulation of apoptotic cell clearance ...regulation of complement activation, alternative pathway / symbiont cell surface / oviduct epithelium development / C5L2 anaphylatoxin chemotactic receptor binding / regulation of triglyceride biosynthetic process / positive regulation of activation of membrane attack complex / complement component C3b binding / regulation of complement-dependent cytotoxicity / vertebrate eye-specific patterning / positive regulation of apoptotic cell clearance / complement-mediated synapse pruning / regulation of complement activation / Alternative complement activation / positive regulation of G protein-coupled receptor signaling pathway / positive regulation of lipid storage / positive regulation of phagocytosis, engulfment / complement receptor mediated signaling pathway / Activation of C3 and C5 / positive regulation of type IIa hypersensitivity / positive regulation of glucose transmembrane transport / complement-dependent cytotoxicity / heparan sulfate proteoglycan binding / serine-type endopeptidase complex / complement activation, alternative pathway / complement activation / neuron remodeling / endopeptidase inhibitor activity / amyloid-beta clearance / positive regulation of vascular endothelial growth factor production / Purinergic signaling in leishmaniasis infection / Peptide ligand-binding receptors / fatty acid metabolic process / complement activation, classical pathway / Regulation of Complement cascade / Post-translational protein phosphorylation / response to bacterium / positive regulation of receptor-mediated endocytosis / positive regulation of angiogenesis / Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs) / Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell / azurophil granule lumen / heparin binding / G alpha (i) signalling events / secretory granule lumen / blood microparticle / inflammatory response / positive regulation of protein phosphorylation / immune response / G protein-coupled receptor signaling pathway / endoplasmic reticulum lumen / signaling receptor binding / Neutrophil degranulation / cell surface / signal transduction / protein-containing complex / proteolysis / extracellular space / extracellular exosome / extracellular region / identical protein binding / plasma membrane Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Kajander, T. / Lehtinen, M.J. / Hyvarinen, S. / Bhattacharjee, A. / Leung, E. / Isenman, D.E. / Meri, S. / Jokiranta, T.S. / Goldman, A. | ||||||
![]() | ![]() Title: Dual Interaction of Factor H with C3D and Glycosaminoglycans in Host-Nonhost Discrimination by Complement. Authors: Kajander, T. / Lehtinen, M.J. / Hyvarinen, S. / Bhattacharjee, A. / Leung, E. / Isenman, D.E. / Meri, S. / Goldman, A. / Jokiranta, T.S. #1: ![]() Title: Structure of Complement Factor H Carboxyl-Terminus Reveals Molecular Basis of Atypical Haemolytic Uremic Syndrome. Authors: Jokiranta, T.S. / Jaakola, V. / Lehtinen, M.J. / Parepalo, M. / Meri, S. / Goldman, A. #2: Journal: J.Biol.Chem. / Year: 2009 Title: Mutations of Factor H Impair Regulation of Surface- Bound C3B by Three Mechanisms in Atypical Hemolytic Uremic Syndrome. Authors: Lehtinen, M.J. / Rops, A.L. / Isenman, D.E. / Van Der Vlag, J. / Jokiranta, T.S. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 153.9 KB | Display | ![]() |
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PDB format | ![]() | 120.9 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 448.5 KB | Display | ![]() |
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Full document | ![]() | 467.5 KB | Display | |
Data in XML | ![]() | 29.1 KB | Display | |
Data in CIF | ![]() | 40.8 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1c3dS ![]() 2hr0 S: Starting model for refinement |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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4 | ![]()
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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS oper: (Code: given Matrix: (0.83692, 0.41801, 0.35331), Vector: |
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Components
#1: Protein | Mass: 32898.734 Da / Num. of mol.: 2 / Fragment: THIOESTER DOMAIN, RESIDUES 996-1287 / Mutation: YES Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() #2: Protein | | Mass: 14984.093 Da / Num. of mol.: 1 / Fragment: DOMAINS 19-20, RESIDUES 1103-1231 / Mutation: YES Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() #3: Water | ChemComp-HOH / | Compound details | ENGINEERED RESIDUE IN CHAIN A, CYS1010 TO ALA ENGINEERED RESIDUE IN CHAIN B, CYS1010 TO ALA ...ENGINEERED | Sequence details | CHAIN A AND B HAVE A POINT MUTATION C17A AND FRAGMENT CRYSTALLIZED HAS RESIDUES N-TERMINAL FROM CD3 ...CHAIN A AND B HAVE A POINT MUTATION C17A AND FRAGMENT CRYSTALLIZ | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.71 Å3/Da / Density % sol: 54.54 % / Description: NONE |
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Crystal grow | Temperature: 295 K / pH: 7.5 Details: 12-18% PEG 4000, 0.1 M HEPES, PH 7.5, AT 22 DEGREES C |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC QUANTUM 315r / Detector: CCD / Date: Jun 29, 2009 / Details: MIRRORS |
Radiation | Monochromator: SI(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.983 Å / Relative weight: 1 |
Reflection | Resolution: 2.3→50 Å / Num. obs: 37791 / % possible obs: 99.7 % / Observed criterion σ(I): -3 / Redundancy: 5.6 % / Biso Wilson estimate: 43.65 Å2 / Rmerge(I) obs: 0.07 / Net I/σ(I): 15.3 |
Reflection shell | Resolution: 2.3→2.44 Å / Redundancy: 5.6 % / Rmerge(I) obs: 0.75 / Mean I/σ(I) obs: 2.36 / % possible all: 98.5 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 1C3D Resolution: 2.306→41.753 Å / SU ML: 0.38 / σ(F): 1.39 / Phase error: 26 / Stereochemistry target values: ML
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 52.214 Å2 / ksol: 0.331 e/Å3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 53.18 Å2
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Refinement step | Cycle: LAST / Resolution: 2.306→41.753 Å
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Refine LS restraints |
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LS refinement shell |
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