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- SASDAF7: Metal-bound hETHE1 (Persulfide dioxygenase ETHE1, mitochondrial, ... -

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Open data


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Basic information

Entry
Database: SASBDB / ID: SASDAF7
SampleMetal-bound hETHE1
  • Persulfide dioxygenase ETHE1, mitochondrial (protein), hETHE1, Homo sapiens
Function / homology
Function and homology information


persulfide dioxygenase / sulfide oxidation / Sulfide oxidation to sulfate / sulfur dioxygenase activity / hydrogen sulfide metabolic process / glutathione metabolic process / iron ion binding / mitochondrial matrix / mitochondrion / identical protein binding ...persulfide dioxygenase / sulfide oxidation / Sulfide oxidation to sulfate / sulfur dioxygenase activity / hydrogen sulfide metabolic process / glutathione metabolic process / iron ion binding / mitochondrial matrix / mitochondrion / identical protein binding / nucleus / cytoplasm
Similarity search - Function
Persulfide dioxygenase-like, MBL-fold metallo-hydrolase domain / : / Metallo-beta-lactamase superfamily / Metallo-beta-lactamase superfamily / Metallo-beta-lactamase / Ribonuclease Z/Hydroxyacylglutathione hydrolase-like
Similarity search - Domain/homology
Persulfide dioxygenase ETHE1, mitochondrial
Similarity search - Component
Biological speciesHomo sapiens (human)
Contact author
  • Al Kikhney
  • Marco Salomone-Stagni

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Models

Model #278
Type: dummy / Software: DAMMIN (5.3) / Radius of dummy atoms: 1.80 A / Symmetry: P2 / Chi-square value: 1.308
Search similar-shape structures of this assembly by Omokage search (details)
Model #287
Type: atomic / Software: CRYSOL (2.8.3) / Chi-square value: 1.352
Search similar-shape structures of this assembly by Omokage search (details)

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Sample

SampleName: Metal-bound hETHE1 / Specimen concentration: 2.00-5.00
BufferName: Tris / Concentration: 50.00 mM / pH: 8
Comment: TCEP does not reduce metals in solution, but prevents aggregation and precipitation of the protein
Composition: 150 mM NaCl 2 mM TCEP
Entity #157Name: hETHE1 / Type: protein / Description: Persulfide dioxygenase ETHE1, mitochondrial / Formula weight: 27.873 / Num. of mol.: 2 / Source: Homo sapiens / References: UniProt: O95571

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Experimental information

BeamInstrument name: DORIS III 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
DetectorName: Pilatus 1M-W / Pixsize x: 0.172 mm
Scan
Title: Metal-bound hETHE1 / Measurement date: Oct 21, 2007 / Cell temperature: 9 °C / Exposure time: 30 sec. / Number of frames: 4 / Unit: 1/nm /
MinMax
Q0.0835 4.981
Distance distribution function P(R)
Sofotware P(R): GNOM 5.0 / Number of points: 1369 /
MinMax
Q0.155228 3.3215
P(R) point1 1369
R0 7.5
Result
Type of curve: merged
Comments: Metal-bound hETHE1 was shown by SAXS to be a globular protein compatible with a dimeric hETHE1 in solution. The calculated scattering pattern from a high resolution model of dimeric ETHE1 ...Comments: Metal-bound hETHE1 was shown by SAXS to be a globular protein compatible with a dimeric hETHE1 in solution. The calculated scattering pattern from a high resolution model of dimeric ETHE1 is in a very good agreement (χ2 value of 1.5) with the experimental data from hETHE1. The low resolution shape of metal-bound hETHE1 was reconstructed ab initio using DAMMIN with P2 symmetry imposed. The ab initio model fits the experimental data with a discrepancy χ2 = 1.3 and is in a good agreement with the high resolution ETHE1 structure.
ExperimentalExperimental errorPorodPorod errorEstimatedEstimated method
MW42 kDa4 42 kDa4 --
Volume--70 nm37 78.87 DAMMIN

P(R)P(R) errorGuinierGuinier error
Forward scattering, I098.52 0.1952 99.96 0.29
Radius of gyration, Rg2.408 nm0.004 2.47 nm0.24

MinMaxError
D-7.5 1
Guinier point32 293 -

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