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- PDB-2ylh: Structure of N-terminal domain of Candida albicans Als9-2 G299W mutant -
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Open data
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Basic information
Entry | Database: PDB / ID: 2ylh | ||||||
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Title | Structure of N-terminal domain of Candida albicans Als9-2 G299W mutant | ||||||
![]() | AGGLUTININ-LIKE PROTEIN | ||||||
![]() | CELL ADHESION / ADHESIN / PEPTIDE-BINDING PROTEIN | ||||||
Function / homology | ![]() cell adhesion involved in multi-species biofilm formation / : / fungal-type cell wall / cell adhesion involved in single-species biofilm formation / cell wall / : / side of membrane / cell adhesion molecule binding / cell-cell adhesion / cell adhesion ...cell adhesion involved in multi-species biofilm formation / : / fungal-type cell wall / cell adhesion involved in single-species biofilm formation / cell wall / : / side of membrane / cell adhesion molecule binding / cell-cell adhesion / cell adhesion / extracellular region / plasma membrane Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Salgado, P.S. / Burchell, L. / Cota, E. | ||||||
![]() | ![]() Title: Structural Basis for the Broad Specificity to Host- Cell Ligands by the Pathogenic Fungus Candida Albicans. Authors: Salgado, P.S. / Yan, R. / Taylor, J.D. / Burchell, L. / Jones, R. / Hoyer, L.L. / Matthews, S.J. / Simpson, P.J. / Cota, E. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 143.9 KB | Display | ![]() |
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PDB format | ![]() | 112.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 2y7lC ![]() 2y7mC ![]() 2y7nSC ![]() 2y7oC C: citing same article ( S: Starting model for refinement |
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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: 33675.098 Da / Num. of mol.: 1 / Fragment: NT_ALS9-2 N-TERMINAL DOMAIN, RESIDUES 18-328 / Mutation: YES Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
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#2: Water | ChemComp-HOH / |
Compound details | ENGINEERED |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.2 Å3/Da / Density % sol: 43.4 % / Description: NONE |
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC QUANTUM 315r / Detector: CCD / Date: May 16, 2010 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.12713 Å / Relative weight: 1 |
Reflection | Resolution: 1.7→33.05 Å / Num. obs: 32813 / % possible obs: 97.8 % / Observed criterion σ(I): 5.5 / Redundancy: 5.2 % / Biso Wilson estimate: 21.917 Å2 / Rmerge(I) obs: 0.06 / Net I/σ(I): 17.4 |
Reflection shell | Resolution: 1.7→1.8 Å / Redundancy: 4.6 % / Rmerge(I) obs: 0.28 / Mean I/σ(I) obs: 5.88 / % possible all: 94.4 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 2Y7N Resolution: 1.7→33.05 Å / Cor.coef. Fo:Fc: 0.941 / Cor.coef. Fo:Fc free: 0.923 / SU B: 5.921 / SU ML: 0.087 / Cross valid method: THROUGHOUT / ESU R: 0.123 / ESU R Free: 0.121 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS.
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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: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 24.019 Å2
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Refinement step | Cycle: LAST / Resolution: 1.7→33.05 Å
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Refine LS restraints |
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