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Open data
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Basic information
Entry | Database: PDB / ID: 1qa1 | ||||||
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Title | TAILSPIKE PROTEIN, MUTANT V331G | ||||||
![]() | TAILSPIKE PROTEIN | ||||||
![]() | Viral protein/receptor / virus/viral protein / Viral protein-receptor COMPLEX | ||||||
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 | ![]() | ||||||
![]() | Baxa, U. / Steinbacher, S. / 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 | ![]() | 144.3 KB | Display | ![]() |
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PDB format | ![]() | 112.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 362.7 KB | Display | ![]() |
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Full document | ![]() | 367 KB | Display | |
Data in XML | ![]() | 11.2 KB | Display | |
Data in CIF | ![]() | 18.2 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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Links
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Assembly
Deposited unit | ![]()
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2 | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 59574.570 Da / Num. of mol.: 1 / Fragment: RECEPTOR BINDING C-TERMINAL DOMAIN / Mutation: V331G 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: 50.22 % | |||||||||||||||
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Crystal grow | Temperature: 274 K / Method: vapor diffusion, hanging drop / pH: 10 Details: VAPOR DIFFUSION, HANGING DROP, 274 K, PH 10.0, 1M AMMONIUM SULPHATE 0.1M NA- PHOSPHATE | |||||||||||||||
Crystal grow | *PLUS Temperature: 4 ℃ / Method: unknown | |||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction source | Source: ![]() |
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Detector | Type: MARRESEARCH / Detector: IMAGE PLATE |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Relative weight: 1 |
Reflection | Resolution: 2→15 Å / Num. all: 39183 / % possible obs: 97.4 % / Redundancy: 3 % / Rmerge(I) obs: 0.041 |
Reflection shell | Resolution: 2→2.05 Å / Rmerge(I) obs: 0.09 / % possible all: 88.7 |
Reflection | *PLUS Num. obs: 39183 / Num. measured all: 115812 |
Reflection shell | *PLUS % possible obs: 88.7 % |
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Processing
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Refinement | Resolution: 2→8 Å / σ(F): 0 / σ(I): 0 / Stereochemistry target values: ENGH & HUBER /
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Refinement step | Cycle: LAST / Resolution: 2→8 Å
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Refine LS restraints |
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Software | *PLUS Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Rfactor all: 0.166 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS |