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- SASDAA6: Human serum albumin monomer and mixtures (Human serum albumin mon... -

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Basic information

Entry
Database: SASBDB / ID: SASDAA6
SampleHuman serum albumin monomer and mixtures
  • Human serum albumin monomer (protein), HSA, Homo sapiens
Function / homology
Function and homology information


exogenous protein binding / Ciprofloxacin ADME / enterobactin binding / cellular response to calcium ion starvation / Heme biosynthesis / HDL remodeling / negative regulation of mitochondrial depolarization / Prednisone ADME / Heme degradation / Aspirin ADME ...exogenous protein binding / Ciprofloxacin ADME / enterobactin binding / cellular response to calcium ion starvation / Heme biosynthesis / HDL remodeling / negative regulation of mitochondrial depolarization / Prednisone ADME / Heme degradation / Aspirin ADME / antioxidant activity / toxic substance binding / Scavenging of heme from plasma / Recycling of bile acids and salts / cellular response to starvation / platelet alpha granule lumen / fatty acid binding / Post-translational protein phosphorylation / Cytoprotection by HMOX1 / Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs) / pyridoxal phosphate binding / Platelet degranulation / protein-folding chaperone binding / blood microparticle / copper ion binding / endoplasmic reticulum lumen / Golgi apparatus / endoplasmic reticulum / protein-containing complex / DNA binding / extracellular space / extracellular exosome / extracellular region / identical protein binding / nucleus / cytoplasm
Similarity search - Function
Serum albumin/Alpha-fetoprotein/Afamin / ALB/AFP/VDB / Serum albumin, N-terminal / Serum albumin, conserved site / Serum albumin-like / Serum albumin family / Albumin domain signature. / Albumin domain profile. / serum albumin
Similarity search - Domain/homology
Biological speciesHomo sapiens (human)
CitationJournal: Nat Methods / Year: 2015
Title: Correlation Map, a goodness-of-fit test for one-dimensional X-ray scattering spectra.
Authors: Daniel Franke / Cy M Jeffries / Dmitri I Svergun /
Abstract: Assessing similarity between data sets with the reduced χ(2) test requires the estimation of experimental errors, which, if incorrect, may render statistical comparisons invalid. We report a ...Assessing similarity between data sets with the reduced χ(2) test requires the estimation of experimental errors, which, if incorrect, may render statistical comparisons invalid. We report a goodness-of-fit test, Correlation Map (CorMap), for assessing differences between one-dimensional spectra independently of explicit error estimates, using only data point correlations. Using small-angle X-ray scattering data, we demonstrate that CorMap maintains the power of the reduced χ(2) test; moreover, CorMap is also applicable to other physical experiments.
Contact author
  • Dmitri Svergun
  • Cy M Jeffries
  • Daniel Franke

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Models

Model #170
Type: dummy / Radius of dummy atoms: 1.90 A / Chi-square value: 0.962361
Search similar-shape structures of this assembly by Omokage search (details)
Model #171
Type: atomic / Comment: ChainA from PDB 1E78 / Chi-square value: 1.010025 / P-value: 0.036000
Search similar-shape structures of this assembly by Omokage search (details)
Model #172
Type: atomic / Comment: ChainB from PDB 1E78 / Chi-square value: 1.0 / P-value: 0.036000
Search similar-shape structures of this assembly by Omokage search (details)

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Sample

SampleName: Human serum albumin monomer and mixtures / Ext coefficient: 0.518 / Purity method: Size exclusion chromatography
BufferName: 50 mM HEPES / Concentration: 50.00 mM / pH: 7.5
Entity #120Name: HSA / Type: protein / Description: Human serum albumin monomer / Formula weight: 66.47 / Num. of mol.: 1 / Source: Homo sapiens / References: UniProt: P02768
Sequence: DAHKSEVAHR FKDLGEENFK ALVLIAFAQY LQQCPFEDHV KLVNEVTEFA KTCVADESAE NCDKSLHTLF GDKLCTVATL RETYGEMADC CAKQEPERNE CFLQHKDDNP NLPRLVRPEV DVMCTAFHDN EETFLKKYLY EIARRHPYFY APELLFFAKR YKAAFTECCQ ...Sequence:
DAHKSEVAHR FKDLGEENFK ALVLIAFAQY LQQCPFEDHV KLVNEVTEFA KTCVADESAE NCDKSLHTLF GDKLCTVATL RETYGEMADC CAKQEPERNE CFLQHKDDNP NLPRLVRPEV DVMCTAFHDN EETFLKKYLY EIARRHPYFY APELLFFAKR YKAAFTECCQ AADKAACLLP KLDELRDEGK ASSAKQRLKC ASLQKFGERA FKAWAVARLS QRFPKAEFAE VSKLVTDLTK VHTECCHGDL LECADDRADL AKYICENQDS ISSKLKECCE KPLLEKSHCI AEVENDEMPA DLPSLAADFV ESKDVCKNYA EAKDVFLGMF LYEYARRHPD YSVVLLLRLA KTYETTLEKC CAAADPHECY AKVFDEFKPL VEEPQNLIKQ NCELFEQLGE YKFQNALLVR YTKKVPQVST PTLVEVSRNL GKVGSKCCKH PEAKRMPCAE DYLSVVLNQL CVLHEKTPVS DRVTKCCTES LVNRRPCFSA LEVDETYVPK EFNAETFTFH ADICTLSEKE RQIKKQTALV ELVKHKPKAT KEQLKAVMDD FAAFVEKCCK ADDKETCFAE EGKKLVAASQ AALGL

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Experimental information

BeamInstrument name: PETRA III P12 / City: Hamburg / 国: Germany / Type of source: X-ray synchrotron / Wavelength: 0.12 Å / Dist. spec. to detc.: 3.1 mm
DetectorName: Pilatus 2M
Scan
Title: Human serum albumin / Measurement date: Jan 22, 2014 / Storage temperature: 20 °C / Unit: 1/nm /
MinMax
Q0.1596 3.3001
Distance distribution function P(R)
Sofotware P(R): GNOM 5.0 / Number of points: 1133 /
MinMax
Q0.159573 3.142
P(R) point1 1133
R0 8.42
Result
Type of curve: single_conc /
ExperimentalPorod
MW61 kDa61 kDa
Volume-103.43 nm3

P(R)Guinier
Forward scattering, I0522.8 521.4
Radius of gyration, Rg2.8 nm2.8 nm

MinMax
D-8.42
Guinier point1 117

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