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Yorodumi- PDB-3sku: Herpes simplex virus glycoprotein D bound to the human receptor n... -
+Open data
-Basic information
Entry | Database: PDB / ID: 3sku | |||||||||
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Title | Herpes simplex virus glycoprotein D bound to the human receptor nectin-1 | |||||||||
Components |
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Keywords | VIRAL PROTEIN/PROTEIN BINDING / Immunoglobulin-like fold / VIRAL PROTEIN-PROTEIN BINDING complex | |||||||||
Function / homology | Function and homology information Nectin/Necl trans heterodimerization / desmosome organization / protein localization to cell junction / lens morphogenesis in camera-type eye / growth cone membrane / enamel mineralization / cell-cell contact zone / Adherens junctions interactions / virion binding / apical junction complex ...Nectin/Necl trans heterodimerization / desmosome organization / protein localization to cell junction / lens morphogenesis in camera-type eye / growth cone membrane / enamel mineralization / cell-cell contact zone / Adherens junctions interactions / virion binding / apical junction complex / heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules / regulation of synapse assembly / homophilic cell adhesion via plasma membrane adhesion molecules / coreceptor activity / presynaptic active zone membrane / cell adhesion molecule binding / hippocampal mossy fiber to CA3 synapse / axon guidance / adherens junction / cell-cell adhesion / retina development in camera-type eye / virus receptor activity / iron ion transport / carbohydrate binding / host cell Golgi apparatus / entry receptor-mediated virion attachment to host cell / cell adhesion / immune response / symbiont entry into host cell / viral envelope / dendrite / protein-containing complex binding / virion membrane / protein homodimerization activity / extracellular region / identical protein binding / membrane / metal ion binding / plasma membrane Similarity search - Function | |||||||||
Biological species | Human herpesvirus 1 (Herpes simplex virus type 1) Homo sapiens (human) | |||||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 4 Å | |||||||||
Authors | Di Giovine, P. / Settembre, E.C. / Bhargava, A.K. / Luftig, M.A. / Lou, H. / Cohen, G.H. / Eisenberg, R.J. / Krummenacher, C. / Carfi, A. | |||||||||
Citation | Journal: Plos Pathog. / Year: 2011 Title: Structure of herpes simplex virus glycoprotein d bound to the human receptor nectin-1. Authors: Di Giovine, P. / Settembre, E.C. / Bhargava, A.K. / Luftig, M.A. / Lou, H. / Cohen, G.H. / Eisenberg, R.J. / Krummenacher, C. / Carfi, A. | |||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 3sku.cif.gz | 520.6 KB | Display | PDBx/mmCIF format |
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PDB format | pdb3sku.ent.gz | 430.8 KB | Display | PDB format |
PDBx/mmJSON format | 3sku.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 3sku_validation.pdf.gz | 2.1 MB | Display | wwPDB validaton report |
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Full document | 3sku_full_validation.pdf.gz | 2.2 MB | Display | |
Data in XML | 3sku_validation.xml.gz | 54.6 KB | Display | |
Data in CIF | 3sku_validation.cif.gz | 71.9 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/sk/3sku ftp://data.pdbj.org/pub/pdb/validation_reports/sk/3sku | HTTPS FTP |
-Related structure data
-Links
-Assembly
Deposited unit |
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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS domain:
NCS domain segments:
NCS ensembles :
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-Components
#1: Protein | Mass: 31624.973 Da / Num. of mol.: 3 / Fragment: UNP residues 26-310 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Human herpesvirus 1 (Herpes simplex virus type 1) Production host: Spodoptera frugiperda (fall armyworm) / References: UniProt: Q991M3 #2: Protein | Mass: 35824.211 Da / Num. of mol.: 3 / Fragment: UNP residues 31-345 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: PVRL1, HVEC, PRR1 / Production host: Spodoptera frugiperda (fall armyworm) / References: UniProt: Q15223 #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: Polysaccharide | Source method: isolated from a genetically manipulated source #5: Sugar | ChemComp-NAG / Has protein modification | Y | |
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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: 4.66 Å3/Da / Density % sol: 73.63 % |
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Crystal grow | Temperature: 293 K / pH: 7.2 Details: 1.0 M Na2HPO4/KH2PO4 pH 7.2 and 300 mM NH4SO4, VAPOR DIFFUSION, temperature 293K |
-Data collection
Diffraction | Mean temperature: 100 K | |||||||||||||||
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Diffraction source | Source: SYNCHROTRON / Site: APS / Beamline: 14-BM-C / Wavelength: 1 | |||||||||||||||
Detector | Type: MAR CCD 165 mm / Detector: CCD / Date: May 14, 2005 | |||||||||||||||
Radiation | Monochromator: SI(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray | |||||||||||||||
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 | |||||||||||||||
Reflection twin |
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Reflection | Resolution: 4→49.1 Å / Num. obs: 31947 / % possible obs: 99.9 % / Observed criterion σ(I): 1 / Redundancy: 2.6 % / Rsym value: 0.06 / Net I/σ(I): 8 | |||||||||||||||
Reflection shell | Resolution: 4→4.1 Å / Redundancy: 2.1 % / Mean I/σ(I) obs: 1.7 / Rsym value: 0.208 / % possible all: 99.2 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 2C36, 1NEU AND 3ALP Resolution: 4→30 Å / Cor.coef. Fo:Fc: 0.885 / Cor.coef. Fo:Fc free: 0.868 / SU B: 100.28 / SU ML: 0.561 / Cross valid method: THROUGHOUT / ESU R Free: 0.142 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: MASK | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 151.77 Å2
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Refinement step | Cycle: LAST / Resolution: 4→30 Å
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Refine LS restraints |
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Refine LS restraints NCS | Refine-ID: X-RAY DIFFRACTION
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