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- PDB-5fs5: Breaking down the wall: mutation of the tyrosine gate of the univ... -
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Open data
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Basic information
Entry | Database: PDB / ID: 5fs5 | |||||||||
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Title | Breaking down the wall: mutation of the tyrosine gate of the universal Escherichia coli fimbrial adhesin FimH | |||||||||
![]() | FIMH | |||||||||
![]() | CELL ADHESION / BACTERIAL ADHESIN / TYPE 1 FIMBRIAE / URINARY TRACT INFECTION / VARIABLE IMMUNOGLOBULIN FOLD | |||||||||
Function / homology | ![]() pilus tip / mechanosensory behavior / cell adhesion involved in single-species biofilm formation / pilus / cell-substrate adhesion / D-mannose binding / host cell membrane / cell adhesion Similarity search - Function | |||||||||
Biological species | ![]() ![]() | |||||||||
Method | ![]() ![]() ![]() | |||||||||
![]() | Bouckaert, J. | |||||||||
![]() | ![]() Title: Mutation of Tyr137 of the universal Escherichia coli fimbrial adhesin FimH relaxes the tyrosine gate prior to mannose binding. Authors: Rabbani, S. / Krammer, E.M. / Roos, G. / Zalewski, A. / Preston, R. / Eid, S. / Zihlmann, P. / Prevost, M. / Lensink, M.F. / Thompson, A. / Ernst, B. / Bouckaert, J. | |||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 117.9 KB | Display | ![]() |
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PDB format | ![]() | 94 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 670.4 KB | Display | ![]() |
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Full document | ![]() | 671.8 KB | Display | |
Data in XML | ![]() | 12.9 KB | Display | |
Data in CIF | ![]() | 19.7 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 4ca4C ![]() 5fwrC ![]() 5fx3C ![]() 4auuS 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 on special symmetry positions |
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Components
#1: Protein | Mass: 16824.732 Da / Num. of mol.: 1 / Fragment: LECTIN DOMAIN, UNP RESIDUES 10-167 / Mutation: YES Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
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#2: Sugar | ChemComp-KGM / |
#3: Chemical | ChemComp-NA / |
#4: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 1.93 Å3/Da / Density % sol: 36.19 % / Description: NONE |
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Crystal grow | pH: 6.5 Details: 5% PGA-LM; 100 MM NA CACODYLATE PH 6.5; 12 % W/V PEG 8K; 10 MM N-HEPTYL ALPHA-D-MANNOPYRANOSIDE |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: RAYONIX / Detector: CCD / Date: Apr 19, 2012 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.91841 Å / Relative weight: 1 |
Reflection | Resolution: 1.42→16.24 Å / Num. obs: 25691 / % possible obs: 98.4 % / Observed criterion σ(I): 1.34 / Redundancy: 6.64 % / Biso Wilson estimate: 8.64 Å2 / Rmerge(I) obs: 0.09 / Net I/σ(I): 17.03 |
Reflection shell | Resolution: 1.42→1.48 Å / Redundancy: 91.8 % / Rmerge(I) obs: 0.47 / Mean I/σ(I) obs: 4.15 / % possible all: 89 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 4AUU Resolution: 1.42→16.246 Å / SU ML: 0.12 / σ(F): 1.34 / Phase error: 14.21 / Stereochemistry target values: ML
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.42→16.246 Å
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Refine LS restraints |
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LS refinement shell |
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