+
Open data
-
Basic information
Entry | Database: PDB / ID: 7zet | ||||||
---|---|---|---|---|---|---|---|
Title | Crystal structure of human Clusterin, crystal form I | ||||||
![]() | Clusterin | ||||||
![]() | CHAPERONE / molecular chaperone / complement system / Alzheimer's disease | ||||||
Function / homology | ![]() immune complex clearance / perinuclear endoplasmic reticulum lumen / regulation of neuronal signal transduction / positive regulation of neurofibrillary tangle assembly / : / central nervous system myelin maintenance / : / response to misfolded protein / negative regulation of response to endoplasmic reticulum stress / spherical high-density lipoprotein particle ...immune complex clearance / perinuclear endoplasmic reticulum lumen / regulation of neuronal signal transduction / positive regulation of neurofibrillary tangle assembly / : / central nervous system myelin maintenance / : / response to misfolded protein / negative regulation of response to endoplasmic reticulum stress / spherical high-density lipoprotein particle / protein carrier chaperone / Terminal pathway of complement / protein targeting to lysosome involved in chaperone-mediated autophagy / chromaffin granule / regulation of amyloid-beta clearance / microglial cell proliferation / misfolded protein binding / apical dendrite / negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage / reverse cholesterol transport / positive regulation of ubiquitin-dependent protein catabolic process / protein import / negative regulation of amyloid fibril formation / complement activation / neurofibrillary tangle / positive regulation of tau-protein kinase activity / Antimicrobial peptides / positive regulation of amyloid fibril formation / low-density lipoprotein particle receptor binding / positive regulation of amyloid-beta formation / negative regulation of release of cytochrome c from mitochondria / negative regulation of amyloid-beta formation / chaperone-mediated protein complex assembly / negative regulation of protein-containing complex assembly / chaperone-mediated protein folding / positive regulation of intrinsic apoptotic signaling pathway / intrinsic apoptotic signaling pathway / release of cytochrome c from mitochondria / platelet alpha granule lumen / complement activation, classical pathway / Regulation of Complement cascade / microglial cell activation / positive regulation of protein-containing complex assembly / response to virus / tau protein binding / cell morphogenesis / lipid metabolic process / positive regulation of receptor-mediated endocytosis / positive regulation of tumor necrosis factor production / positive regulation of nitric oxide biosynthetic process / unfolded protein binding / positive regulation of proteasomal ubiquitin-dependent protein catabolic process / Platelet degranulation / positive regulation of NF-kappaB transcription factor activity / amyloid-beta binding / regulation of cell population proliferation / protein-folding chaperone binding / regulation of apoptotic process / collagen-containing extracellular matrix / negative regulation of neuron apoptotic process / mitochondrial inner membrane / protein stabilization / blood microparticle / positive regulation of apoptotic process / protein heterodimerization activity / intracellular membrane-bounded organelle / innate immune response / signaling receptor binding / synapse / ubiquitin protein ligase binding / protein-containing complex binding / positive regulation of gene expression / perinuclear region of cytoplasm / Golgi apparatus / cell surface / protein-containing complex / mitochondrion / extracellular space / extracellular exosome / extracellular region / nucleus / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() ![]() | ||||||
![]() | Yuste-Checa, P. / Bracher, A. / Hartl, F.U. | ||||||
Funding support | 1items
| ||||||
![]() | ![]() Title: Crystal structure of human Clusterin, crystal form I Authors: Yuste-Checa, P. / Bracher, A. / Hartl, F.U. | ||||||
History |
|
-
Structure visualization
Structure viewer | Molecule: ![]() ![]() |
---|
-
Downloads & links
-
Download
PDBx/mmCIF format | ![]() | 95.2 KB | Display | ![]() |
---|---|---|---|---|
PDB format | ![]() | 69.5 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 947.9 KB | Display | ![]() |
---|---|---|---|---|
Full document | ![]() | 949.7 KB | Display | |
Data in XML | ![]() | 15 KB | Display | |
Data in CIF | ![]() | 19.4 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar structure data | Similarity search - Function & homology ![]() |
---|
-
Links
-
Assembly
Deposited unit | ![]()
| ||||||||
---|---|---|---|---|---|---|---|---|---|
1 |
| ||||||||
2 |
| ||||||||
Unit cell |
|
-
Components
#1: Protein | Mass: 47038.852 Da / Num. of mol.: 1 / Fragment: Clu-delta(214-238) / Mutation: deletion(214-238) Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() | ||
---|---|---|---|
#2: Polysaccharide | 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose Source method: isolated from a genetically manipulated source | ||
#3: Polysaccharide | beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta- ...beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose Source method: isolated from a genetically manipulated source | ||
#4: Sugar | ChemComp-NAG / Has ligand of interest | N | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
---|
-
Sample preparation
Crystal | Density Matthews: 3 Å3/Da / Density % sol: 59.07 % / Mosaicity: 0.25 ° |
---|---|
Crystal grow | Temperature: 277 K / Method: vapor diffusion, sitting drop / pH: 5.6 Details: 30% PEG-4000, 0.2 M NH4-acetate, 0.1 M Na-citrate pH 5.6 |
-Data collection
Diffraction | Mean temperature: 100 K / Serial crystal experiment: N | ||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Diffraction source | Source: ![]() ![]() ![]() | ||||||||||||||||||||||||||||||
Detector | Type: DECTRIS EIGER X 16M / Detector: PIXEL / Date: Dec 2, 2021 | ||||||||||||||||||||||||||||||
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray | ||||||||||||||||||||||||||||||
Radiation wavelength | Wavelength: 0.7749 Å / Relative weight: 1 | ||||||||||||||||||||||||||||||
Reflection | Resolution: 2.8→49.08 Å / Num. obs: 13861 / % possible obs: 98.2 % / Redundancy: 3.7 % / Biso Wilson estimate: 75.02 Å2 / CC1/2: 0.995 / Rmerge(I) obs: 0.146 / Rpim(I) all: 0.088 / Rrim(I) all: 0.172 / Net I/σ(I): 5.9 / Num. measured all: 50668 / Scaling rejects: 4 | ||||||||||||||||||||||||||||||
Reflection shell | Diffraction-ID: 1
|
-Phasing
Phasing | Method: ![]() | ||||||
---|---|---|---|---|---|---|---|
Phasing MR | R rigid body: 0.596
|
-
Processing
Software |
| ||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method to determine structure: ![]() Starting model: AlphaFold AF-P10909-F1-model_v1.pdb Resolution: 2.8→27.61 Å / SU ML: 0.54 / Cross valid method: THROUGHOUT / σ(F): 1.34 / Phase error: 35.41 / Stereochemistry target values: ML Details: The Clusterin construct is a glyco-protein, which was expressed in the presence of the alpha-mannosidase I inhibitor kifunensine, which prevents trimming of mannose moieties, resulting in ...Details: The Clusterin construct is a glyco-protein, which was expressed in the presence of the alpha-mannosidase I inhibitor kifunensine, which prevents trimming of mannose moieties, resulting in oligo-mannose N-glycans, and thereby prevents processing to mature complex N-glycans (Chang et al., Structure 15, 267(2007), Fig. 1B). Asn residues 86, 103, 145, 291, 354 and 374 are expected to carry predominantly NAG-NAG-BMA-(3->1)MAN-MAN-MAN (6->1)-MAN (3->1)MAN-MAN (6->1)MAN-MAN N-glycan trees (Chang et al., Structure 15, 267(2007), Fig. 1B).
| ||||||||||||||||||||||||||||||||||||||||||
Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL | ||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso max: 161.13 Å2 / Biso mean: 80.9892 Å2 / Biso min: 36.33 Å2 | ||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: final / Resolution: 2.8→27.61 Å
| ||||||||||||||||||||||||||||||||||||||||||
LS refinement shell | Refine-ID: X-RAY DIFFRACTION / Rfactor Rfree error: 0 / Total num. of bins used: 5
|