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Open data
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Basic information
| Entry | Database: SASBDB / ID: SASDA32 |
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Sample | BSA in HEPES
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| Function / homology | Function and homology informationcellular response to calcium ion starvation / enterobactin binding / negative regulation of mitochondrial depolarization / toxic substance binding / fatty acid binding / cellular response to starvation / pyridoxal phosphate binding / protein-containing complex / extracellular space / DNA binding ...cellular response to calcium ion starvation / enterobactin binding / negative regulation of mitochondrial depolarization / toxic substance binding / fatty acid binding / cellular response to starvation / pyridoxal phosphate binding / protein-containing complex / extracellular space / DNA binding / extracellular region / metal ion binding / cytoplasm Similarity search - Function |
| Biological species | ![]() |
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Structure visualization
| Structure viewer | Molecule: Molmil Jmol/JSmol |
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Downloads & links
-Data source
| SASBDB page | SASDA32 |
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-Related structure data
| Similar structure data |
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External links
| Related items in Molecule of the Month |
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-Models
| Model #4 | ![]() Type: dummy / Radius of dummy atoms: 1.80 A / Symmetry: P1 / Chi-square value: 2.566404 Search similar-shape structures of this assembly by Omokage search (details) |
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| Model #3 | ![]() Type: atomic / Software: (28) Search similar-shape structures of this assembly by Omokage search (details) |
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Sample
Sample | Name: BSA in HEPES / Ext coefficient: 6.46 / Contrast: 2.953 / Specific vol: 0.737 / Purity method: gel filtration / Dry vol: 17570 / Sample MW: 66 kDa / Specimen concentration: 25.64 mg/ml / Concentration method: nanodrop |
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| Buffer | Name: 50 mM HEPES 50 mM KCl / Concentration: 50.00 mM / PK: 7 / pH: 7.5 / Comment: 4-(2-hydroxyethyl)-1-piperazineethanesulfonic acid / Composition: KCl 50.000 mM |
| Entity #1 | Name: BSA / Type: protein / Description: Serum albumin / Formula weight: 69.29 / Num. of mol.: 1 / Source: Bos taurus / References: UniProt: P02769 Sequence: MKWVTFISLL LLFSSAYSRG VFRRDTHKSE IAHRFKDLGE EHFKGLVLIA FSQYLQQCPF DEHVKLVNEL TEFAKTCVAD ESHAGCEKSL HTLFGDELCK VASLRETYGD MADCCEKQEP ERNECFLSHK DDSPDLPKLK PDPNTLCDEF KADEKKFWGK YLYEIARRHP ...Sequence: MKWVTFISLL LLFSSAYSRG VFRRDTHKSE IAHRFKDLGE EHFKGLVLIA FSQYLQQCPF DEHVKLVNEL TEFAKTCVAD ESHAGCEKSL HTLFGDELCK VASLRETYGD MADCCEKQEP ERNECFLSHK DDSPDLPKLK PDPNTLCDEF KADEKKFWGK YLYEIARRHP YFYAPELLYY ANKYNGVFQE CCQAEDKGAC LLPKIETMRE KVLASSARQR LRCASIQKFG ERALKAWSVA RLSQKFPKAE FVEVTKLVTD LTKVHKECCH GDLLECADDR ADLAKYICDN QDTISSKLKE CCDKPLLEKS HCIAEVEKDA IPENLPPLTA DFAEDKDVCK NYQEAKDAFL GSFLYEYSRR HPEYAVSVLL RLAKEYEATL EECCAKDDPH ACYSTVFDKL KHLVDEPQNL IKQNCDQFEK LGEYGFQNAL IVRYTRKVPQ VSTPTLVEVS RSLGKVGTRC CTKPESERMP CTEDYLSLIL NRLCVLHEKT PVSEKVTKCC TESLVNRRPC FSALTPDETY VPKAFDEKLF TFHADICTLP DTEKQIKKQT ALVELLKHKP KATEEQLKTV MENFVAFVDK CCAADDKEAC FAVEGPKLVV STQTALA |
-Experimental information
| Beam | Instrument name: DORIS III EMBL X33 / City: Hamburg / 国: Germany / Shape: 0.6 / Type of source: X-ray synchrotron / Wavelength: 0.15 Å / Dist. spec. to detc.: 2.7 mm | ||||||||||||||||||||||||||||||
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| Detector | Name: Pilatus 1M-W / Pixsize x: 0.172 mm | ||||||||||||||||||||||||||||||
| Scan |
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| Distance distribution function P(R) |
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| Result | Comments: Bovin Serum Albumin (BSA) is an extremely important protein in Small Angle X-Ray Scattering. It is, in fact, used as standard in order to calculate the molecular weight of other proteins. ...Comments: Bovin Serum Albumin (BSA) is an extremely important protein in Small Angle X-Ray Scattering. It is, in fact, used as standard in order to calculate the molecular weight of other proteins. The reasons why it has been chosen as standard it is because it can be easily stored in its powder form and it is also very well characterised. In solution is present as a monomer-dimer equilibrium, therefore the molecular weight of the standard BSA is not the one of the monomer (68 kDa) but is slightly bigger (72 kDa). The crystal structure of BSA has been solved recently therefore ab initio models can be compared with atomic structure like in this picture.
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