+Open data
-Basic information
Entry | Database: SASBDB / ID: SASDCK3 |
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Sample | aldehyde dehydrogenase
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Function / homology | Function and homology information acetaldehyde dehydrogenase (acetylating) / acetaldehyde dehydrogenase (acetylating) activity / alcohol metabolic process / carbon utilization / alcohol dehydrogenase (NAD+) activity / alcohol dehydrogenase / metal ion binding Similarity search - Function |
Biological species | Escherichia coli O157:H7 (bacteria) |
Contact author |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Data source
SASBDB page | SASDCK3 |
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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 #1260 | Type: dummy / Radius of dummy atoms: 2.40 A / Symmetry: P1 / Chi-square value: 1.774 Search similar-shape structures of this assembly by Omokage search (details) |
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Model #1261 | Type: dummy / Software: (5.0 r9217) / Radius of dummy atoms: 2.50 A / Symmetry: P1 / Comment: this is the averaged representation of the model / Chi-square value: 1.774 / P-value: 0.459900 Search similar-shape structures of this assembly by Omokage search (details) |
-Sample
Sample | Name: aldehyde dehydrogenase / Specimen concentration: 2 mg/ml |
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Buffer | Name: 30 mM HEPES, 150 mM NaCl, 5% (v/v) glycerol / pH: 7.5 |
Entity #603 | Name: AdhE / Type: protein / Description: Aldehyde-alcohol dehydrogenase / Formula weight: 48.038 / Num. of mol.: 1 / Source: Escherichia coli O157:H7 / References: UniProt: P0A9Q8 Sequence: MAVTNVAELN ALVERVKKAQ REYASFTQEQ VDKIFRAAAL AAADARIPLA KMAVAESGMG IVEDKVIKNH FASEYIYNAY KDEKTCGVLS EDDTFGTITI AEPIGIICGI VPTTNPTSTA IFKSLISLKT RNAIIFSPHP RAKDATNKAA DIVLQAAIAA GAPKDLIGWI ...Sequence: MAVTNVAELN ALVERVKKAQ REYASFTQEQ VDKIFRAAAL AAADARIPLA KMAVAESGMG IVEDKVIKNH FASEYIYNAY KDEKTCGVLS EDDTFGTITI AEPIGIICGI VPTTNPTSTA IFKSLISLKT RNAIIFSPHP RAKDATNKAA DIVLQAAIAA GAPKDLIGWI DQPSVELSNA LMHHPDINLI LATGGPGMVK AAYSSGKPAI GVGAGNTPVV IDETADIKRA VASVLMSKTF DNGVICASEQ SVVVVDSVYD AVRERFATHG GYLLQGKELK AVQDVILKNG ALNAAIVGQP AYKIAELAGF SVPENTKILI GEVTVVDESE PFAHEKLSPT LAMYRAKDFE DAVEKAEKLV AMGGIGHTSC LYTDQDNQPA RVSYFGQKMK TARILINTPA SQGGIGDLYN FKLAPSLTLG CGSWGGNSIS ENVGPKHLIN KKTVAHHHHH H |
-Experimental information
Beam | Instrument name: Diamond Light Source B21 / City: Oxfordshire / 国: UK / Shape: 1 x 5 mm / Type of source: X-ray synchrotron / Wavelength: 0.1 Å / Dist. spec. to detc.: 4.04 mm | |||||||||||||||||||||||||||||||||
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Detector | Name: Pilatus 2M | |||||||||||||||||||||||||||||||||
Scan | Title: Aldehyde dehydrogenase / Measurement date: Jan 30, 2017 / Storage temperature: 4 °C / Cell temperature: 4 °C / Exposure time: 1 sec. / Number of frames: 18 / Unit: 1/A /
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Distance distribution function P(R) | Sofotware P(R): GNOM 5.0 / Number of points: 1264 /
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Result | Type of curve: single_conc Comments: Aldehyde dehydrogenase (AldDH) is the N-terminal domain of the bifunctional alcohol/aldehyde dehydrogenase (AdhE; SASBDB entry SASDC72) spanning amino acids 1-445 of the full-length protein. ...Comments: Aldehyde dehydrogenase (AldDH) is the N-terminal domain of the bifunctional alcohol/aldehyde dehydrogenase (AdhE; SASBDB entry SASDC72) spanning amino acids 1-445 of the full-length protein. SAXS data were measured from a protein construct that included a C-terminal 6 x histidine affinity chromatography tag. The buffer subtraction was performed using Scatter. Subsequent analysis was performed using PRIMUS (ATSAS 2.7.1).
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