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- PDB-2ls2: 1H Chemical Shift Assignments for the first transmembrane domain ... -

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Basic information

Entry
Database: PDB / ID: 2ls2
Title1H Chemical Shift Assignments for the first transmembrane domain from human copper transport 1
ComponentsHigh affinity copper uptake protein 1
KeywordsMETAL TRANSPORT / hCtr1 TMDs / oligomerization
Function / homology
Function and homology information


silver ion transmembrane transporter activity / plasma membrane copper ion transport / silver ion transmembrane transport / Metal ion SLC transporters / copper ion import / copper ion transmembrane transporter activity / vascular endothelial growth factor receptor-2 signaling pathway / copper ion transport / xenobiotic transport / protein complex oligomerization ...silver ion transmembrane transporter activity / plasma membrane copper ion transport / silver ion transmembrane transport / Metal ion SLC transporters / copper ion import / copper ion transmembrane transporter activity / vascular endothelial growth factor receptor-2 signaling pathway / copper ion transport / xenobiotic transport / protein complex oligomerization / xenobiotic transmembrane transporter activity / intercalated disc / intracellular copper ion homeostasis / establishment of localization in cell / recycling endosome membrane / late endosome membrane / early endosome membrane / basolateral plasma membrane / angiogenesis / apical plasma membrane / copper ion binding / identical protein binding / plasma membrane
Similarity search - Function
Ctr copper transporter / Ctr copper transporter family
Similarity search - Domain/homology
High affinity copper uptake protein 1
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodSOLUTION NMR / torsion angle dynamics
Model detailsclosest to the average, model1
AuthorsYang, L. / Huang, Z. / Li, F.
CitationJournal: To be Published
Title: Structural insights into the transmembrane domains of human copper transporter 1
Authors: Yang, L. / Huang, Z. / Li, F.
History
DepositionApr 20, 2012Deposition site: BMRB / Processing site: PDBJ
Revision 1.0Jun 6, 2012Provider: repository / Type: Initial release
Revision 1.1Jun 14, 2023Group: Data collection / Database references / Other
Category: database_2 / pdbx_database_status ...database_2 / pdbx_database_status / pdbx_nmr_spectrometer / struct_ref_seq_dif
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.status_code_nmr_data / _pdbx_nmr_spectrometer.model / _struct_ref_seq_dif.details
Revision 1.2May 15, 2024Group: Data collection / Database references / Category: chem_comp_atom / chem_comp_bond / database_2 / Item: _database_2.pdbx_DOI

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: High affinity copper uptake protein 1


Theoretical massNumber of molelcules
Total (without water)2,6811
Polymers2,6811
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)20 / 200target function
RepresentativeModel #1closest to the average

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Components

#1: Protein/peptide High affinity copper uptake protein 1 / Copper transporter 1 / hCTR1 / Solute carrier family 31 member 1


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

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
1112D 1H-1H NOESY
1212D 1H-1H TOCSY
NMR detailsText: 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

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Sample preparation

DetailsContents: 2 mM TMD1-1, 40% hexafluoroisopropanol (HFIP) aqueous solution
Solvent system: 40% hexafluoroisopropanol (HFIP) aqueous solution
SampleConc.: 2 mM / Component: TMD1-1
Sample conditionsPressure: ambient / Temperature: 298 K

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NMR measurement

NMR spectrometerType: Bruker Avance / Manufacturer: Bruker / Model: AVANCE / Field strength: 500 MHz

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Processing

NMR softwareName: CYANA / Developer: Glntert P. / Classification: refinement
RefinementMethod: torsion angle dynamics / Software ordinal: 1
NMR representativeSelection criteria: closest to the average
NMR ensembleConformer selection criteria: target function / Conformers calculated total number: 200 / Conformers submitted total number: 20 / Representative conformer: 1

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