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Open data
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Basic information
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| Title | CryoEM structure of LARGE1 from C1 reconstruction | ||||||||||||
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Sample |
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Keywords | Glycosyltransferase / Metalloenzyme / TRANSFERASE | ||||||||||||
| Function / homology | Function and homology informationDefective LARGE causes MDDGA6 and MDDGB6 / xylosyltransferase activity / skeletal muscle organ development / glucuronosyltransferase activity / Matriglycan biosynthesis on DAG1 / Transferases; Glycosyltransferases / UDP-xylosyltransferase activity / protein O-linked glycosylation via mannose / glycosphingolipid biosynthetic process / negative regulation of muscle cell apoptotic process ...Defective LARGE causes MDDGA6 and MDDGB6 / xylosyltransferase activity / skeletal muscle organ development / glucuronosyltransferase activity / Matriglycan biosynthesis on DAG1 / Transferases; Glycosyltransferases / UDP-xylosyltransferase activity / protein O-linked glycosylation via mannose / glycosphingolipid biosynthetic process / negative regulation of muscle cell apoptotic process / positive regulation of skeletal muscle acetylcholine-gated channel clustering / N-acetylglucosamine metabolic process / acetylglucosaminyltransferase activity / hexosyltransferase activity / protein O-linked glycosylation / skeletal muscle tissue regeneration / glycoprotein biosynthetic process / muscle cell cellular homeostasis / Transferases; Glycosyltransferases; Hexosyltransferases / glycosyltransferase activity / Transferases; Glycosyltransferases; Pentosyltransferases / positive regulation of Rac protein signal transduction / neuromuscular junction / manganese ion binding / positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction / Golgi membrane / Golgi apparatus / protein-containing complex / plasma membrane Similarity search - Function | ||||||||||||
| Biological species | Homo sapiens (human) | ||||||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 3.7 Å | ||||||||||||
Authors | Joseph S / Schnicker NJ / Campbell KP | ||||||||||||
| Funding support | United States, 3 items
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Citation | Journal: To Be PublishedTitle: CryoEM structure of LARGE1 from C1 reconstruction Authors: Campbell KP | ||||||||||||
| History |
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Structure visualization
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Downloads & links
-EMDB archive
| Map data | emd_26540.map.gz | 91.7 MB | EMDB map data format | |
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| Header (meta data) | emd-26540-v30.xml emd-26540.xml | 15.8 KB 15.8 KB | Display Display | EMDB header |
| Images | emd_26540.png | 196.5 KB | ||
| Filedesc metadata | emd-26540.cif.gz | 5.8 KB | ||
| Others | emd_26540_half_map_1.map.gz emd_26540_half_map_2.map.gz | 95.6 MB 95.6 MB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-26540 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-26540 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 7ui6MC 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_26540.map.gz / Format: CCP4 / Size: 103 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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| Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
| Voxel size | X=Y=Z: 0.8015 Å | ||||||||||||||||||||||||||||||||||||
| Density |
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
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-Supplemental data
-Half map: #2
| File | emd_26540_half_map_1.map | ||||||||||||
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| Projections & Slices |
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| Density Histograms |
-Half map: #1
| File | emd_26540_half_map_2.map | ||||||||||||
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| Density Histograms |
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Sample components
-Entire : LARGE1
| Entire | Name: LARGE1 |
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| Components |
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-Supramolecule #1: LARGE1
| Supramolecule | Name: LARGE1 / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1 / Details: No transmembrane region |
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| Source (natural) | Organism: Homo sapiens (human) |
| Molecular weight | Theoretical: 211 KDa |
-Macromolecule #1: Xylosyl- and glucuronyltransferase LARGE1
| Macromolecule | Name: Xylosyl- and glucuronyltransferase LARGE1 / type: protein_or_peptide / ID: 1 / Number of copies: 2 / Enantiomer: LEVO / EC number: Transferases; Glycosyltransferases |
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| Source (natural) | Organism: Homo sapiens (human) |
| Molecular weight | Theoretical: 89.806242 KDa |
| Recombinant expression | Organism: Homo sapiens (human) |
| Sequence | String: MSALLILALV GAAVADYKDH DGDYKDHDID YKDDDDKLAA AFEDGKPVSL SPLESQAHSP RYTASSQRER ESLEVRMREV EEENRALRR QLSLAQGRAP SHRRGNHSKT YSMEEGTGDS ENLRAGIVAG NSSECGQQPV VEKCETIHVA IVCAGYNASR D VVTLVKSV ...String: MSALLILALV GAAVADYKDH DGDYKDHDID YKDDDDKLAA AFEDGKPVSL SPLESQAHSP RYTASSQRER ESLEVRMREV EEENRALRR QLSLAQGRAP SHRRGNHSKT YSMEEGTGDS ENLRAGIVAG NSSECGQQPV VEKCETIHVA IVCAGYNASR D VVTLVKSV LFHRRNPLHF HLIADSIAEQ ILATLFQTWM VPAVRVDFYN ADELKSEVSW IPNKHYSGIY GLMKLVLTKT LP ANLERVI VLDTDITFAT DIAELWAVFH KFKGQQVLGL VENQSDWYLG NLWKNHRPWP ALGRGYNTGV ILLLLDKLRK MKW EQMWRL TAERELMGML STSLADQDIF NAVIKQNPFL VYQLPCFWNV QLSDHTRSEQ CYRDVSDLKV IHWNSPKKLR VKNK HVEFF RNLYLTFLEY DGNLLRRELF GCPSEADVNS ENLQKQLSEL DEDDLCYEFR RERFTVHRTH LYFLHYEYEP AADST DVTL VAQLSMDRLQ MLEAICKHWE GPISLALYLS DAEAQQFLRY AQGSEVLMSR HNVGYHIVYK EGQFYPVNLL RNVAMK HIS TPYMFLSDID FLPMYGLYEY LRKSVIQLDL ANTKKAMIVP AFETLRYRLS FPKSKAELLS MLDMGTLFTF RYHVWTK GH APTNFAKWRT ATTPYRVEWE ADFEPYVVVR RDCPEYDRRF VGFGWNKVAH IMELDVQEYE FIVLPNAYMI HMPHAPSF D ITKFRSNKQY RICLKTLKEE FQQDMSRRYG FAALKYLTAE NNSHHHHHH UniProtKB: Xylosyl- and glucuronyltransferase LARGE1 |
-Macromolecule #2: MANGANESE (II) ION
| Macromolecule | Name: MANGANESE (II) ION / type: ligand / ID: 2 / Number of copies: 4 / Formula: MN |
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| Molecular weight | Theoretical: 54.938 Da |
-Experimental details
-Structure determination
| Method | cryo EM |
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Processing | single particle reconstruction |
| Aggregation state | particle |
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Sample preparation
| Concentration | 0.5 mg/mL |
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| Buffer | pH: 6.6 |
| Grid | Model: UltrAuFoil R2/2 / Material: GOLD / Mesh: 200 |
| Vitrification | Cryogen name: ETHANE / Instrument: FEI VITROBOT MARK IV |
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Electron microscopy
| Microscope | TFS KRIOS |
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| Image recording | Film or detector model: GATAN K3 (6k x 4k) / Average exposure time: 1.664 sec. / Average electron dose: 50.0 e/Å2 |
| Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
| Electron optics | C2 aperture diameter: 70.0 µm / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal defocus max: 2.0 µm / Nominal defocus min: 0.8 µm |
| 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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Image processing
-Atomic model buiding 1
| Details | Used initial model from Alphafold2 |
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| Refinement | Space: REAL / Protocol: AB INITIO MODEL |
| Output model | ![]() PDB-7ui6: |
Movie
Controller
About Yorodumi




Keywords
Homo sapiens (human)
Authors
United States, 3 items
Citation


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




































FIELD EMISSION GUN
