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Open data
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Basic information
Entry | Database: PDB / ID: 1clw | ||||||
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Title | TAILSPIKE PROTEIN FROM PHAGE P22, V331A MUTANT | ||||||
![]() | TAILSPIKE PROTEIN | ||||||
![]() | VIRAL PROTEIN / LATE PROTEIN / VIRUS/VIRAL PROTEIN | ||||||
Function / homology | ![]() endo-1,3-alpha-L-rhamnosidase activity / symbiont entry into host cell via disruption of host cell envelope lipopolysaccharide / virus tail, fiber / symbiont entry into host cell via disruption of host cell envelope / symbiont entry into host / Hydrolases; Glycosylases; Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl compounds / adhesion receptor-mediated virion attachment to host cell / metabolic process / virion attachment to host cell Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() | ||||||
![]() | Steinbacher, S. / Baxa, U. / Weintraub, A. / Huber, R. / Seckler, R. | ||||||
![]() | ![]() Title: Mutations improving the folding of phage P22 tailspike protein affect its receptor binding activity. Authors: Baxa, U. / Steinbacher, S. / Weintraub, A. / Huber, R. / Seckler, R. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 118.8 KB | Display | ![]() |
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PDB format | ![]() | 89.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 363.7 KB | Display | ![]() |
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Full document | ![]() | 368.3 KB | Display | |
Data in XML | ![]() | 11.2 KB | Display | |
Data in CIF | ![]() | 18.3 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1qa1C ![]() 1qa2C ![]() 1qa3C ![]() 1tspS 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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Unit cell |
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Components
#1: Protein | Mass: 59588.594 Da / Num. of mol.: 1 / Fragment: CATALYTIC FRAGMENT / Mutation: V331A Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
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#2: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.47 Å3/Da / Density % sol: 50.21 % | |||||||||||||||
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Crystal grow | pH: 10 / Details: pH 10.00 | |||||||||||||||
Crystal grow | *PLUS Temperature: 4 ℃ / pH: 10 / Method: vapor diffusion | |||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 288 K |
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Diffraction source | Source: ![]() |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE |
Radiation | Monochromator: GRAPHITE / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2→8 Å / Num. obs: 40008 / % possible obs: 99.5 % / Redundancy: 3.2 % / Rmerge(I) obs: 0.068 / Rsym value: 0.068 |
Reflection shell | Resolution: 2→2.05 Å / Rmerge(I) obs: 0.157 / Rsym value: 0.157 / % possible all: 93.6 |
Reflection | *PLUS Num. measured all: 128481 / Rmerge(I) obs: 0.068 |
Reflection shell | *PLUS % possible obs: 93.6 % / Rmerge(I) obs: 0.157 |
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Processing
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Refinement | Method to determine structure: OTHER Starting model: 1TSP Resolution: 2→8 Å / Isotropic thermal model: RESTRAINED / σ(F): 0
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Refinement step | Cycle: LAST / Resolution: 2→8 Å
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Refine LS restraints |
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Refinement | *PLUS Highest resolution: 2 Å / Lowest resolution: 8 Å / Rfactor obs: 0.171 / Rfactor Rwork: 0.171 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS Type: x_angle_deg / Dev ideal: 1.6 |