Heme-binding Protein A; Chain: A; / Haem-binding HasA / Haem-binding HasA / Haem-binding HasA superfamily / Heme-binding protein A (HasA) / 2-Layer Sandwich / Alpha Beta Similarity search - Domain/homology
SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN ... SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW, TWO SHEETS ARE DEFINED.
Mass: 18.015 Da / Num. of mol.: 149 / Source method: isolated from a natural source / Formula: H2O
Compound details
IT IS CAPABLE OF BINDING FREE HEME AS WELL AS CAN ACQUIRE IT FROM THE HEMOGLOBIN.IT IS REPONSIBLE ...IT IS CAPABLE OF BINDING FREE HEME AS WELL AS CAN ACQUIRE IT FROM THE HEMOGLOBIN.IT IS REPONSIBLE FOR TRANSFERRING HEME FROM HEMOGLOB TO THE HASR RECEPTOR WHICH RELEASES IT INTO THE BACTERIUM.
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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: 2.17 Å3/Da / Density % sol: 43 %
Crystal grow
pH: 8.5 Details: 2 MICROLITERS PROTEIN (AT A CONCENTRATION OF ABOUT 4 MG/ML) WERE MIXED WITH 1 MICROLITER RESERVOIR CONSISTING OF 100 MM TRIS BUFFER AT PH 8.5, 2 M K2HPO4 AND 2 M NAH2PO4.
Resolution: 2.3→30 Å / Cor.coef. Fo:Fc: 0.939 / Cor.coef. Fo:Fc free: 0.889 / SU B: 4.185 / SU ML: 0.105 / Cross valid method: THROUGHOUT / ESU R: 0.492 / ESU R Free: 0.246 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS.
Rfactor
Num. reflection
% reflection
Selection details
Rfree
0.224
676
5 %
RANDOM
Rwork
0.169
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obs
0.172
12866
95.3 %
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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: BABINET MODEL WITH MASK