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Yorodumi- PDB-2ls2: 1H Chemical Shift Assignments for the first transmembrane domain ... -
+Open data
-Basic information
Entry | Database: PDB / ID: 2ls2 | ||||||
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Title | 1H Chemical Shift Assignments for the first transmembrane domain from human copper transport 1 | ||||||
Components | High affinity copper uptake protein 1 | ||||||
Keywords | METAL TRANSPORT / hCtr1 TMDs / oligomerization | ||||||
Function / homology | Function and homology information silver ion transmembrane transporter activity / plasma membrane copper ion transport / Metal ion SLC transporters / silver ion transmembrane transport / copper ion transmembrane transporter activity / copper ion import / vascular endothelial growth factor receptor-2 signaling pathway / copper ion transport / xenobiotic transport / xenobiotic transmembrane transporter activity ...silver ion transmembrane transporter activity / plasma membrane copper ion transport / Metal ion SLC transporters / silver ion transmembrane transport / copper ion transmembrane transporter activity / copper ion import / vascular endothelial growth factor receptor-2 signaling pathway / copper ion transport / xenobiotic transport / xenobiotic transmembrane transporter activity / intercalated disc / intracellular copper ion homeostasis / establishment of localization in cell / recycling endosome membrane / protein complex oligomerization / late endosome membrane / early endosome membrane / basolateral plasma membrane / angiogenesis / apical plasma membrane / copper ion binding / identical protein binding / plasma membrane Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | SOLUTION NMR / torsion angle dynamics | ||||||
Model details | closest to the average, model1 | ||||||
Authors | Yang, L. / Huang, Z. / Li, F. | ||||||
Citation | Journal: To be Published Title: Structural insights into the transmembrane domains of human copper transporter 1 Authors: Yang, L. / Huang, Z. / Li, F. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2ls2.cif.gz | 127.7 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2ls2.ent.gz | 89.2 KB | Display | PDB format |
PDBx/mmJSON format | 2ls2.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2ls2_validation.pdf.gz | 445.3 KB | Display | wwPDB validaton report |
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Full document | 2ls2_full_validation.pdf.gz | 626.2 KB | Display | |
Data in XML | 2ls2_validation.xml.gz | 28.9 KB | Display | |
Data in CIF | 2ls2_validation.cif.gz | 28.3 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ls/2ls2 ftp://data.pdbj.org/pub/pdb/validation_reports/ls/2ls2 | HTTPS FTP |
-Related structure data
Related structure data | 2ls3C 2ls4C C: citing same article (ref.) |
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Similar structure data | Similarity search - Function & homologyF&H Search |
Other databases |
-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein/peptide | Mass: 2681.175 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: SLC31A1, COPT1, CTR1 / Production host: Escherichia coli (E. coli) / References: UniProt: O15431 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||
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NMR experiment |
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NMR details | Text: the TOCSY spectra were recorded with mixing time of 100 ms. The NOESY spectra were recorded with mixing times 200 ms. The WATERGATE technique was used in both experiments for water suppression |
-Sample preparation
Details | Contents: 2 mM TMD1-1, 40% hexafluoroisopropanol (HFIP) aqueous solution Solvent system: 40% hexafluoroisopropanol (HFIP) aqueous solution |
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Sample | Conc.: 2 mM / Component: TMD1-1 |
Sample conditions | Pressure: ambient / Temperature: 298 K |
-NMR measurement
NMR spectrometer | Type: Bruker Avance / Manufacturer: Bruker / Model: AVANCE / Field strength: 500 MHz |
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-Processing
NMR software | Name: CYANA / Developer: Glntert P. / Classification: refinement |
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Refinement | Method: torsion angle dynamics / Software ordinal: 1 |
NMR representative | Selection criteria: closest to the average |
NMR ensemble | Conformer selection criteria: target function / Conformers calculated total number: 200 / Conformers submitted total number: 20 / Representative conformer: 1 |