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- PDB-2c36: Structure of unliganded HSV gD reveals a mechanism for receptor- ... -
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Open data
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Basic information
Entry | Database: PDB / ID: 2c36 | ||||||||||||
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Title | Structure of unliganded HSV gD reveals a mechanism for receptor- mediated activation of virus entry | ||||||||||||
![]() | GLYCOPROTEIN D HSV-1 | ||||||||||||
![]() | VIRAL PROTEIN / VIRUS / HERPES / IMMUNOGLOBULIN-LIKE / GLYCOPROTEIN / TRANSMEMBRANE | ||||||||||||
Function / homology | ![]() host cell Golgi apparatus / entry receptor-mediated virion attachment to host cell / symbiont entry into host cell / viral envelope / virion membrane / membrane / metal ion binding Similarity search - Function | ||||||||||||
Biological species | ![]() ![]() | ||||||||||||
Method | ![]() ![]() ![]() | ||||||||||||
![]() | Krummenacher, C. / Supekar, V.M. / Whitbeck, J.C. / Lazear, E. / Connolly, S.A. / Eisenberg, R.J. / Cohen, G.H. / Wiley, D.C. / Carfi, A. | ||||||||||||
![]() | ![]() Title: Structure of unliganded HSV gD reveals a mechanism for receptor-mediated activation of virus entry. Authors: Krummenacher, C. / Supekar, V.M. / Whitbeck, J.C. / Lazear, E. / Connolly, S.A. / Eisenberg, R.J. / Cohen, G.H. / Wiley, D.C. / Carfi, A. | ||||||||||||
History |
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Remark 700 | SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN ... SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW, TWO SHEETS ARE DEFINED. |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 136.9 KB | Display | ![]() |
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PDB format | ![]() | 105.8 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 1.3 MB | Display | ![]() |
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Full document | ![]() | 1.3 MB | Display | |
Data in XML | ![]() | 28.3 KB | Display | |
Data in CIF | ![]() | 42 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 2c3aC ![]() 1l2gS S: Starting model for refinement C: citing same article ( |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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1 | ![]()
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2 | ![]()
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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS oper: (Code: given Matrix: (0.92906, 0.01627, 0.36958), Vector: |
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Components
-Protein , 1 types, 2 molecules AB
#1: Protein | Mass: 31558.824 Da / Num. of mol.: 2 / Mutation: YES Source method: isolated from a genetically manipulated source Details: N-ACETYL-GLUCOSAMINE LINKED TO ASN121 AND ASN94 IN BOTH SUBUNITS (CHAIN A, B) Source: (gene. exp.) ![]() ![]() Strain: PATTON / Plasmid: PRSVNT / Cell line (production host): SF9 / Production host: ![]() ![]() |
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-Sugars , 2 types, 3 molecules
#2: Polysaccharide | 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 |
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-Non-polymers , 3 types, 513 molecules ![](data/chem/img/ZN.gif)
![](data/chem/img/CL.gif)
![](data/chem/img/HOH.gif)
![](data/chem/img/CL.gif)
![](data/chem/img/HOH.gif)
#4: Chemical | ChemComp-ZN / | ||
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#5: Chemical | #6: Water | ChemComp-HOH / | |
-Details
Compound details | ENGINEERED |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.8 Å3/Da / Density % sol: 67.2 % |
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Crystal grow | pH: 6 Details: 0.1M NA-CACODYLATE PH 6.0, 100MM NACL, 100UM ZNAC2, 20% PEG 4K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC CCD / Detector: CCD / Date: Sep 12, 2004 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 2.1→81.65 Å / Num. obs: 55770 / % possible obs: 92.5 % / Observed criterion σ(I): 2 / Redundancy: 4.3 % / Rmerge(I) obs: 0.06 / Net I/σ(I): 14.4 |
Reflection shell | Resolution: 2.1→2.18 Å / Redundancy: 3.9 % / Rmerge(I) obs: 0.42 / Mean I/σ(I) obs: 2.8 / % possible all: 78.1 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 1L2G Resolution: 2.11→81.65 Å / Cor.coef. Fo:Fc: 0.957 / Cor.coef. Fo:Fc free: 0.933 / SU B: 4.808 / SU ML: 0.119 / Cross valid method: THROUGHOUT / ESU R: 0.164 / ESU R Free: 0.166 / Stereochemistry target values: MAXIMUM LIKELIHOOD Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. DISORDERED REGION FROM RESIDUE 257 TO 267 FOR BOTH CHAINS
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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: BABINET MODEL WITH MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 40.85 Å2
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Refinement step | Cycle: LAST / Resolution: 2.11→81.65 Å
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Refine LS restraints |
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