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- PDB-1bct: THREE-DIMENSIONAL STRUCTURE OF PROTEOLYTIC FRAGMENT 163-231 OF BA... -

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Entry
Database: PDB / ID: 1bct
TitleTHREE-DIMENSIONAL STRUCTURE OF PROTEOLYTIC FRAGMENT 163-231 OF BACTERIOOPSIN DETERMINED FROM NUCLEAR MAGNETIC RESONANCE DATA IN SOLUTION
ComponentsBACTERIORHODOPSIN
KeywordsPHOTORECEPTOR
Function / homology
Function and homology information


photoreceptor activity / phototransduction / proton transmembrane transport / monoatomic ion channel activity / plasma membrane
Similarity search - Function
Bacteriorhodopsin Fragment / Bacteriorhodopsin Fragment / Bacterial rhodopsins retinal binding site. / Bacterial rhodopsins signature 1. / Rhodopsin, retinal binding site / Bacteriorhodopsin-like protein / Archaeal/bacterial/fungal rhodopsins / Bacteriorhodopsin-like protein / Few Secondary Structures / Irregular
Similarity search - Domain/homology
Biological speciesHalobacterium salinarum (Halophile)
MethodSOLUTION NMR
AuthorsNolde, D.E. / Barsukov, I.L. / Lomize, A.L. / Arseniev, A.S.
Citation
Journal: Eur.J.Biochem. / Year: 1992
Title: Three-dimensional structure of proteolytic fragment 163-231 of bacterioopsin determined from nuclear magnetic resonance data in solution.
Authors: Barsukov, I.L. / Nolde, D.E. / Lomize, A.L. / Arseniev, A.S.
#1: Journal: Eur.J.Biochem. / Year: 1990
Title: Sequence-Specific 1H (Slash)NMR Assignment and Conformation of Proteolytic Fragment 163-231 of Bacterioopsin
Authors: Barsukov, I.L. / Abdulaeva, G.V. / Arseniev, A.S. / Bystrov, V.F.
History
DepositionJul 7, 1993Processing site: BNL
Revision 1.0Apr 30, 1994Provider: repository / Type: Initial release
Revision 1.1Mar 24, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Feb 16, 2022Group: Database references / Derived calculations / Other
Category: database_2 / pdbx_database_status ...database_2 / pdbx_database_status / pdbx_struct_assembly / pdbx_struct_oper_list
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.process_site

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Structure viewerMolecule:
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Assembly

Deposited unit
A: BACTERIORHODOPSIN


Theoretical massNumber of molelcules
Total (without water)7,5381
Polymers7,5381
Non-polymers00
Water0
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Atom site foot note1: MET 163 - ARG 164 MODEL 14 OMEGA =210.41 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)14 / -
Representative

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Components

#1: Protein BACTERIORHODOPSIN /


Mass: 7538.013 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Halobacterium salinarum (Halophile) / References: UniProt: P02945

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR

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Sample preparation

Crystal grow
*PLUS
Method: other / Details: NMR

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Processing

NMR ensembleConformers submitted total number: 14

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