response to biotic stimulus / abscisic acid binding / abscisic acid-activated signaling pathway / protein phosphatase inhibitor activity / defense response / signaling receptor activity Similarity search - Function
Pathogenesis-related proteins Bet v I family signature. / Bet v I type allergen / Bet v I/Major latex protein / Pathogenesis-related protein Bet v 1 family / START domain / Alpha-D-Glucose-1,6-Bisphosphate; Chain A, domain 4 / START-like domain superfamily / 2-Layer Sandwich / Alpha Beta Similarity search - Domain/homology
THE PROTEIN IS MONOMERIC IN SOLUTION, BUT FORMS DIMERS IN THE CRYSTAL STRUCTURE VIA ANTIPARALLEL INTERMOLECULAR BETA-SHEETS INVOLVING STRANDS BETA1. THE PAIRING SCHEME IS AB, CD, ..., YZ,...
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Components
#1: Protein
... Phenolicoxidativecouplingprotein / Phenolic oxidative coupling protein Hyp-1
Mass: 18495.109 Da / Num. of mol.: 28 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Hypericum perforatum (plant) / Gene: hyp-1, HYP1.1 / Plasmid: pET151/D / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: Q8H1L1
Mass: 18.015 Da / Num. of mol.: 35 / Source method: isolated from a natural source / Formula: H2O
Sequence details
RESIDUES NUMBERED -5 TO 0 ARE FROM A CLONING ARTIFACT. RESIDUES 1-159 ARE FROM THE GENUINE PROTEIN ...RESIDUES NUMBERED -5 TO 0 ARE FROM A CLONING ARTIFACT. RESIDUES 1-159 ARE FROM THE GENUINE PROTEIN SEQUENCE. THE AMINO ACID SEQUENCE OF THE PRESENT PROTEIN DIFFERS FROM THE DEPOSITED SEQUENCE Q8H1L1 POSSIBLY BECAUSE OF GENETIC VARIABILITY
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Experimental details
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Experiment
Experiment
Method: X-RAY DIFFRACTION / Number of used crystals: 1
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Sample preparation
Crystal
Density Matthews: 3.08 Å3/Da / Density % sol: 60.12 %
Crystal grow
Temperature: 292 K / Method: vapor diffusion, hanging drop / pH: 7.5 Details: HEPES 0.1 M, tribasic sodium citrate 1.3 M, glycerol 10% , pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 292K
Resolution: 2.43→48.87 Å / Cor.coef. Fo:Fc: 0.94 / Cor.coef. Fo:Fc free: 0.933 / Cross valid method: R-FREE / σ(F): 0 / ESU R: 0.078 / ESU R Free: 0.058 / Stereochemistry target values: MAXIMUM LIKELIHOOD Details: HYDROGEN ATOMS WERE ADDED AT RIDING POSITIONS. The reflection data set for refinement in monoclinic symmetry was obtained by expansion of a tetartohedrally twinned data set merged in tetragonal symmetry
Rfactor
Num. reflection
% reflection
Selection details
Rfree
0.27759
3077
1.3 %
RANDOM
Rwork
0.22278
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obs
0.22353
232268
99.7 %
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Solvent computation
Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK