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- PDB-2ls3: 1H Chemical Shift Assignments for the secondary transmembrane dom... -

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Basic information

Entry
Database: PDB / ID: 2ls3
Title1H Chemical Shift Assignments for the secondary 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 / 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 / protein complex oligomerization / 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)3,5401
Polymers3,5401
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: 3540.393 Da / Num. of mol.: 1 / Fragment: UNP RESIDUES 132-157
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

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Sample preparation

DetailsContents: 2 mM hCtr1-TMD2-1, 40% hexafluoroisopropanol (HFIP) aqueous solution
Solvent system: 40% hexafluoroisopropanol (HFIP) aqueous solution
SampleConc.: 2 mM / Component: hCtr1-TMD2-1
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: Gntert, 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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