+Open data
-Basic information
Entry | Database: PDB / ID: 3lnf | ||||||
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Title | Crystal structure of E-cadherin EC12 K14EW2A | ||||||
Components | Cadherin-1 | ||||||
Keywords | CELL ADHESION / cadherin / Calcium / Cell junction / Cell membrane / Glycoprotein / Transmembrane | ||||||
Function / homology | Function and homology information uterine epithelium development / Apoptotic cleavage of cell adhesion proteins / regulation of branching involved in salivary gland morphogenesis / salivary gland cavitation / regulation of protein catabolic process at postsynapse, modulating synaptic transmission / RHO GTPases activate IQGAPs / Adherens junctions interactions / Degradation of the extracellular matrix / regulation of neuron migration / Integrin cell surface interactions ...uterine epithelium development / Apoptotic cleavage of cell adhesion proteins / regulation of branching involved in salivary gland morphogenesis / salivary gland cavitation / regulation of protein catabolic process at postsynapse, modulating synaptic transmission / RHO GTPases activate IQGAPs / Adherens junctions interactions / Degradation of the extracellular matrix / regulation of neuron migration / Integrin cell surface interactions / positive regulation of cell-cell adhesion / lateral loop / gamma-catenin binding / cell-cell adhesion mediated by cadherin / negative regulation of axon extension / regulation of protein localization to cell surface / trophectodermal cell differentiation / alpha-catenin binding / cellular response to indole-3-methanol / flotillin complex / Schmidt-Lanterman incisure / epithelial cell morphogenesis / bicellular tight junction assembly / intestinal epithelial cell development / calcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules / node of Ranvier / protein metabolic process / catenin complex / cell-cell junction assembly / negative regulation of protein processing / negative regulation of protein localization to plasma membrane / GTPase activating protein binding / adherens junction organization / apical junction complex / ankyrin binding / cochlea development / negative regulation of cell-cell adhesion / cellular response to lithium ion / homophilic cell adhesion via plasma membrane adhesion molecules / microvillus / decidualization / canonical Wnt signaling pathway / lateral plasma membrane / establishment of skin barrier / axon terminus / embryo implantation / synapse assembly / protein tyrosine kinase binding / cytoskeletal protein binding / cell adhesion molecule binding / negative regulation of cell migration / cell periphery / protein localization to plasma membrane / cellular response to amino acid stimulus / sensory perception of sound / adherens junction / cell morphogenesis / trans-Golgi network / negative regulation of canonical Wnt signaling pathway / cytoplasmic side of plasma membrane / cell-cell adhesion / beta-catenin binding / positive regulation of protein import into nucleus / regulation of protein localization / negative regulation of epithelial cell proliferation / cell-cell junction / actin cytoskeleton / apical part of cell / lamellipodium / cell junction / actin cytoskeleton organization / postsynapse / regulation of gene expression / basolateral plasma membrane / protein phosphatase binding / in utero embryonic development / molecular adaptor activity / endosome / cadherin binding / axon / protein domain specific binding / glutamatergic synapse / calcium ion binding / perinuclear region of cytoplasm / positive regulation of DNA-templated transcription / cell surface / membrane / identical protein binding / plasma membrane / cytoplasm Similarity search - Function | ||||||
Biological species | Mus musculus (house mouse) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.5 Å | ||||||
Authors | Jin, X. / Harrison, O. / Shapiro, L. | ||||||
Citation | Journal: Nat.Struct.Mol.Biol. / Year: 2010 Title: Two-step adhesive binding by classical cadherins. Authors: Harrison, O.J. / Bahna, F. / Katsamba, P.S. / Jin, X. / Brasch, J. / Vendome, J. / Ahlsen, G. / Carroll, K.J. / Price, S.R. / Honig, B. / Shapiro, L. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 3lnf.cif.gz | 96 KB | Display | PDBx/mmCIF format |
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PDB format | pdb3lnf.ent.gz | 72.5 KB | Display | PDB format |
PDBx/mmJSON format | 3lnf.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ln/3lnf ftp://data.pdbj.org/pub/pdb/validation_reports/ln/3lnf | HTTPS FTP |
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-Related structure data
Related structure data | 3lndC 3lneC 3lngC 3lnhC 3lniC 1edhS C: citing same article (ref.) S: Starting model for refinement |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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2 |
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Unit cell |
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-Components
#1: Protein | Mass: 23145.668 Da / Num. of mol.: 2 / Fragment: UNP residues 157-369 / Mutation: K14E,W2A Source method: isolated from a genetically manipulated source Source: (gene. exp.) Mus musculus (house mouse) / Gene: Cdh1 / Production host: Escherichia coli (E. coli) / References: UniProt: P09803 #2: Chemical | ChemComp-CA / #3: 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: 2.94 Å3/Da / Density % sol: 58.19 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 8.5 Details: 1.2M ammonium sulfate, 0.1M Tris-Cl pH 8.5, 15% (v/v) glycerol, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: NSLS / Beamline: X4A / Wavelength: 0.97897 Å |
Detector | Type: ADSC QUANTUM 4 / Detector: CCD / Date: Feb 16, 2008 |
Radiation | Monochromator: Si 111 CHANNEL / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.97897 Å / Relative weight: 1 |
Reflection | Resolution: 2.5→50 Å / Num. all: 17934 / Num. obs: 17683 / % possible obs: 98.6 % / Observed criterion σ(F): 1 / Observed criterion σ(I): 1 / Redundancy: 2.5 % / Rmerge(I) obs: 0.111 / Net I/σ(I): 8.2 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 1EDH Resolution: 2.5→28.635 Å / SU ML: 0.36 / σ(F): 1.97 / 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: 21.401 Å2 / ksol: 0.369 e/Å3 | |||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.5→28.635 Å
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Refine LS restraints |
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LS refinement shell |
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