PDB entry 1m0l

BACTERIORHODOPSIN/LIPID COMPLEX AT 1.47 A RESOLUTION

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The structure was published by Schobert, B., Cupp-Vickery, J., Hornak, V., Smith, S., and Lanyi, J., in 2002 in a paper entitled "Crystallographic structure of the K intermediate of bacteriorhodopsin: conservation of free energy after photoisomerization of the retinal." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 1.47 Å and deposited in 2002.

The experimental data on which the structure is based was not deposited.

The PDB entry contains the structure of BACTERIORHODOPSIN. This molecule has the UniProt identifier P02945 (BACR_HALSA). The sample contained 262 residues which is 100% of the natural sequence. Out of 262 residues 222 were observed and are deposited in the PDB.

It also contains one or more heterogenic compounds (e.g., ligands, co-factors, ions, modified amino acids, etc.); see here for a complete list.

The molecule most likely forms homotrimers.

The following tables show cross-reference information to other databases (to obtain a list of all PDB entries sharing the same property or classification, click on the magnifying glass icon):

Chain	Name	UniProt	Name of source organism	% of UniProt sequence present in the sample	Residues in the sample molecules	% of residues observed
A	BACTERIORHODOPSIN	P02945 (1-262) (BACR_HALSA)	Halobacterium sp. NRC-1	91%	262	84%

This entry contains 1 unique UniProt protein:

UniProt accession	Name	Organism	PDB
P02945 (1 - 262)	BACTERIORHODOPSIN	Halobacterium salinarum	Related PDB sequences UniProt coverage

Chain	Structural classification (SCOP)	Structural classification (CATH)	Sequence family (Pfam)
A (P02945)	Bacteriorhodopsin-like	Rhopdopsin 7-helix transmembrane proteins	Bacteriorhodopsin-like protein

Chain ID	Molecular function (GO)	Cellular component (GO)	Biological process (GO)
A (P02945)	Receptor activity, Ion channel activity, Photoreceptor activity	Plasma membrane, Membrane, Integral to membrane	Transport, Ion transport, Phototransduction, Proton transport, Protein-chromophore linkage, Response to stimulus

Chain	InterPro annotation
A	Rhodopsin, archaeal/bacterial/fungal, Rhodopsin, retinal binding site