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Open data
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Basic information
| Entry | ![]() | |||||||||
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| Title | Pex5-Eci1 complex - Pex5 local refinement | |||||||||
Map data | Pex5 local refinement | |||||||||
Sample |
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Keywords | Peroxisome / protein targeting / PTS1 / PROTEIN TRANSPORT | |||||||||
| Function / homology | Function and homology informationBeta-oxidation of very long chain fatty acids / peroxisome matrix targeting signal-1 binding / Pexophagy / peroxisomal importomer complex / protein import into peroxisome matrix / Delta3-Delta2-enoyl-CoA isomerase / protein import into peroxisome matrix, docking / delta(3)-delta(2)-enoyl-CoA isomerase activity / Peroxisomal protein import / protein carrier chaperone ...Beta-oxidation of very long chain fatty acids / peroxisome matrix targeting signal-1 binding / Pexophagy / peroxisomal importomer complex / protein import into peroxisome matrix / Delta3-Delta2-enoyl-CoA isomerase / protein import into peroxisome matrix, docking / delta(3)-delta(2)-enoyl-CoA isomerase activity / Peroxisomal protein import / protein carrier chaperone / E3 ubiquitin ligases ubiquitinate target proteins / peroxisomal membrane / fatty acid beta-oxidation / peroxisomal matrix / peroxisome / protein-macromolecule adaptor activity / cytosol Similarity search - Function | |||||||||
| Biological species | ![]() | |||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 2.9 Å | |||||||||
Authors | Elad N / Dym O | |||||||||
| Funding support | European Union, Israel, 2 items
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Citation | Journal: To Be PublishedTitle: An unconventional interaction interface between the peroxisomal targeting factor Pex5 and Eci1 enables PTS1 independent import Authors: Peer L / Elad N / Dym O / Tirosh A / Jacobovitch J / Albeck S / Schuldiner M / Peleg Y / Zalckvar E | |||||||||
| History |
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Structure visualization
| Supplemental images |
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Downloads & links
-EMDB archive
| Map data | emd_50435.map.gz | 125.5 MB | EMDB map data format | |
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| Header (meta data) | emd-50435-v30.xml emd-50435.xml | 22.4 KB 22.4 KB | Display Display | EMDB header |
| FSC (resolution estimation) | emd_50435_fsc.xml | 14.9 KB | Display | FSC data file |
| Images | emd_50435.png | 95.5 KB | ||
| Masks | emd_50435_msk_1.map | 244.1 MB | Mask map | |
| Filedesc metadata | emd-50435.cif.gz | 6.6 KB | ||
| Others | emd_50435_additional_1.map.gz emd_50435_half_map_1.map.gz emd_50435_half_map_2.map.gz | 122.3 MB 226.8 MB 226.8 MB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-50435 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-50435 | HTTPS FTP |
-Validation report
| Summary document | emd_50435_validation.pdf.gz | 1.2 MB | Display | EMDB validaton report |
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| Full document | emd_50435_full_validation.pdf.gz | 1.2 MB | Display | |
| Data in XML | emd_50435_validation.xml.gz | 22 KB | Display | |
| Data in CIF | emd_50435_validation.cif.gz | 28.3 KB | Display | |
| Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-50435 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-50435 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 9fh0MC ![]() 9fgzC M: atomic model generated by this map C: citing same article ( |
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| Similar structure data | Similarity search - Function & homology F&H Search |
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Links
| EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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| Related items in Molecule of the Month |
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Map
| File | Download / File: emd_50435.map.gz / Format: CCP4 / Size: 244.1 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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| Annotation | Pex5 local refinement | ||||||||||||||||||||||||||||||||||||
| Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
| Voxel size | X=Y=Z: 0.842 Å | ||||||||||||||||||||||||||||||||||||
| Density |
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
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-Supplemental data
-Mask #1
| File | emd_50435_msk_1.map | ||||||||||||
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| Projections & Slices |
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| Density Histograms |
-Additional map: Pex5 local refinement unfiltered map
| File | emd_50435_additional_1.map | ||||||||||||
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| Annotation | Pex5 local refinement unfiltered map | ||||||||||||
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| Density Histograms |
-Half map: Pex5 local refinement half map A
| File | emd_50435_half_map_1.map | ||||||||||||
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| Annotation | Pex5 local refinement half map A | ||||||||||||
| Projections & Slices |
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| Density Histograms |
-Half map: Pex5 local refinement half map B
| File | emd_50435_half_map_2.map | ||||||||||||
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| Annotation | Pex5 local refinement half map B | ||||||||||||
| Projections & Slices |
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| Density Histograms |
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Sample components
-Entire : Pex5-Eci1 complex
| Entire | Name: Pex5-Eci1 complex |
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| Components |
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-Supramolecule #1: Pex5-Eci1 complex
| Supramolecule | Name: Pex5-Eci1 complex / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all |
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| Source (natural) | Organism: ![]() |
-Macromolecule #1: 3,2-trans-enoyl-CoA isomerase
| Macromolecule | Name: 3,2-trans-enoyl-CoA isomerase / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO |
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| Source (natural) | Organism: ![]() |
| Molecular weight | Theoretical: 31.736408 KDa |
| Recombinant expression | Organism: ![]() |
| Sequence | String: MSQEIRQNEK ISYRIEGPFF IIHLMNPDNL NALEGEDYIY LGELLELADR NRDVYFTIIQ SSGRFFSSGA DFKGIAKAQG DDTNKYPSE TSKWVSNFVA RNVYVTDAFI KHSKVLICCL NGPAIGLSAA LVALCDIVYS INDKVYLLYP FANLGLITEG G TTVSLPLK ...String: MSQEIRQNEK ISYRIEGPFF IIHLMNPDNL NALEGEDYIY LGELLELADR NRDVYFTIIQ SSGRFFSSGA DFKGIAKAQG DDTNKYPSE TSKWVSNFVA RNVYVTDAFI KHSKVLICCL NGPAIGLSAA LVALCDIVYS INDKVYLLYP FANLGLITEG G TTVSLPLK FGTNTTYECL MFNKPFKYDI MCENGFISKN FNMPSSNAEA FNAKVLEELR EKVKGLYLPS CLGMKKLLKS NH IDAFNKA NSVEVNESLK YWVDGEPLKR FRQLGSKQRK HRL UniProtKB: 3,2-trans-enoyl-CoA isomerase |
-Macromolecule #2: Peroxisomal targeting signal receptor
| Macromolecule | Name: Peroxisomal targeting signal receptor / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO |
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| Source (natural) | Organism: ![]() |
| Molecular weight | Theoretical: 69.335766 KDa |
| Recombinant expression | Organism: Escherichia phage EcSzw-2 (virus) |
| Sequence | String: ADVGSCSVGN NPLAQLHKHT QQNKSLQFNQ KNNGRLNESP LQGTNKPGIS EAFISNVNAI SQENMANMQR FINGEPLIDD KRRMEIGPS SGRLPPFSNV HSLQTSANPT QIKGVNDISH WSQEFQGSNS IQNRNADTGN SEKAWQRGST TASSRFQYPN T MMNNYAYA ...String: ADVGSCSVGN NPLAQLHKHT QQNKSLQFNQ KNNGRLNESP LQGTNKPGIS EAFISNVNAI SQENMANMQR FINGEPLIDD KRRMEIGPS SGRLPPFSNV HSLQTSANPT QIKGVNDISH WSQEFQGSNS IQNRNADTGN SEKAWQRGST TASSRFQYPN T MMNNYAYA SMNSLSGSRL QSPAFMNQQQ SGRSKEGVNE QEQQPWTDQF EKLEKEVSEN LDINDEIEKE ENVSEVEQNK PE TVEKEEG VYGDQYQSDF QEVWDSIHKD AEEVLPSELV NDDLNLGEDY LKYLGGRVNG NIEYAFQSNN EYFNNPNAYK IGC LLMENG AKLSEAALAF EAAVKEKPDH VDAWLRLGLV QTQNEKELNG ISALEECLKL DPKNLEAMKT LAISYINEGY DMSA FTMLD KWAETKYPEI WSRIKQQDDK FQKEKGFTHI DMNAHITKQF LQLANNLSTI DPEIQLCLGL LFYTKDDFDK TIDCF ESAL RVNPNDELMW NRLGASLANS NRSEEAIQAY HRALQLKPSF VRARYNLAVS SMNIGCFKEA AGYLLSVLSM HEVNTN NKK GDVGSLLNTY NDTVIETLKR VFIAMNRDDL LQEVKPGMDL KRFKGEFSF UniProtKB: Peroxisomal targeting signal receptor |
-Experimental details
-Structure determination
| Method | cryo EM |
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Processing | single particle reconstruction |
| Aggregation state | particle |
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Sample preparation
| Buffer | pH: 7.5 |
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| Grid | Model: C-flat-1.2/1.3 / Material: GOLD / Mesh: 300 / Pretreatment - Type: GLOW DISCHARGE / Pretreatment - Time: 90 sec. / Pretreatment - Atmosphere: AIR |
| Vitrification | Cryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 277 K / Instrument: FEI VITROBOT MARK IV |
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Electron microscopy
| Microscope | FEI TITAN KRIOS |
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| Specialist optics | Energy filter - Name: GIF Bioquantum / Energy filter - Slit width: 15 eV |
| Image recording | Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Number grids imaged: 1 / Number real images: 5577 / Average exposure time: 1.6 sec. / Average electron dose: 45.5 e/Å2 |
| Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
| Electron optics | C2 aperture diameter: 70.0 µm / Calibrated magnification: 59382 / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal defocus max: 15.0 µm / Nominal defocus min: 2.7 µm / Nominal magnification: 105000 |
| Sample stage | Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN |
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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About Yorodumi




Keywords
Authors
Israel, 2 items
Citation







Z (Sec.)
Y (Row.)
X (Col.)





















































Escherichia phage EcSzw-2 (virus)
Processing
FIELD EMISSION GUN

