+Open data
-Basic information
Entry | Database: PDB / ID: 1qa3 | ||||||
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Title | TAILSPIKE PROTEIN, MUTANT A334I | ||||||
Components | TAILSPIKE PROTEIN | ||||||
Keywords | Viral protein/receptor / virus/viral protein / Viral protein-receptor COMPLEX | ||||||
Function / homology | Function and homology information 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 | Enterobacteria phage P22 (virus) | ||||||
Method | X-RAY DIFFRACTION / Resolution: 2 Å | ||||||
Authors | Baxa, U. / Steinbacher, S. / Weintraub, A. / Huber, R. / Seckler, R. | ||||||
Citation | Journal: J.Mol.Biol. / Year: 1999 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: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1qa3.cif.gz | 118.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1qa3.ent.gz | 89.9 KB | Display | PDB format |
PDBx/mmJSON format | 1qa3.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/qa/1qa3 ftp://data.pdbj.org/pub/pdb/validation_reports/qa/1qa3 | HTTPS FTP |
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-Related 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: 59658.727 Da / Num. of mol.: 1 / Fragment: RECEPTOR BINDING C-TERMINAL FRAGMENT / Mutation: A334I Source method: isolated from a genetically manipulated source Source: (gene. exp.) Enterobacteria phage P22 (virus) / Genus: P22-like viruses / References: UniProt: P12528 |
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#2: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.47 Å3/Da / Density % sol: 50.15 % | |||||||||||||||
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Crystal grow | Temperature: 277 K / Method: vapor diffusion, hanging drop / pH: 10 Details: VAPOR DIFFUSION, HANGING DROP, 277K, PH 10.0, 1M AMMONIUM SULPHATE 0.1M NA- PHOSPHATE | |||||||||||||||
Crystal grow | *PLUS Temperature: 4 ℃ / Method: vapor diffusion | |||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 287 K |
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Diffraction source | Source: ROTATING ANODE / Type: RIGAKU RU200 |
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: 39240 / Num. obs: 39240 / % possible obs: 98.4 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 3.1 % / Rmerge(I) obs: 0.071 |
Reflection shell | Resolution: 2→2.05 Å / Rmerge(I) obs: 0.224 / % possible all: 90.8 |
Reflection | *PLUS Num. measured all: 121311 |
Reflection shell | *PLUS % possible obs: 90.8 % |
-Processing
Software |
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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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