4X1H: Rhodopsin

Opsin/G(alpha) peptide complex stabilized by nonyl-glucoside. Determined by X-ray diffraction at 2.29 Å resolution. Released 4 Nov 2015.

Method
X-ray diffraction
Resolution
2.29 Å
Organism
Bos taurus
Chains
2
Atoms
2,940
Mol. weight
42.55 kDa
Ligands
BNG, PLM
Released
4 Nov 2015

Explore 4X1H in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4X1H contains 19 α-helices and 4 β-strands across 2 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 18 helices, 4 β-strands

ElementResiduesLengthSheet
β-strand4-631
β-strand9-1131
α-helix34-6431
α-helix66-683
α-helix71-733
α-helix74-8613
α-helix87-915
α-helix92-987
α-helix106-14035
α-helix150-16819
α-helix170-1723
β-strand178-18142
β-strand186-18942
α-helix196-1983
α-helix200-2089
α-helix209-2135
α-helix214-23522
α-helix241-27737
α-helix285-29612
α-helix298-3036
α-helix304-3085
α-helix311-32111
Chain C: 1 helix, 0 β-strands
ElementResiduesLengthSheet
α-helix341-3466

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
RhodopsinAprotein348Bos taurusP02699 (AlphaFold model)
C-terminal derived peptide of guanine nucleotide-binding protein G(t) subunit alpha-1Cprotein11Bos taurus
Sequence of entity 1 (A), FASTA
>4X1H_1 Rhodopsin (chains A)
MNGTEGPNFYVPFSNKTGVVRSPFEAPQYYLAEPWQFSMLAAYMFLLIMLGFPINFLTLY
VTVQHKKLRTPLNYILLNLAVADLFMVFGGFTTTLYTSLHGYFVFGPTGCNLEGFFATLG
GEIALWSLVVLAIERYVVVCKPMSNFRFGENHAIMGVAFTWVMALACAAPPLVGWSRYIP
EGMQCSCGIDYYTPHEETNNESFVIYMFVVHFIIPLIVIFFCYGQLVFTVKEAAAQQQES
ATTQKAEKEVTRMVIIMVIAFLICWLPYAGVAFYIFTHQGSDFGPIFMTIPAFFAKTSAV
YNPVIYIMMNKQFRNCMVTTLCCGKNPLGDDEASTTVSKTETSQVAPA
Sequence of entity 2 (C), FASTA
>4X1H_2 C-terminal derived peptide of guanine nucleotide-binding protein G(t) subunit alpha-1 (chains C)
VLEDLKSCGLF

Ligands and cofactors

IDNameFormulaCopies
BNGnonyl beta-D-glucopyranosideC15 H30 O62
PLMPalmitic acidC16 H32 O22

Primary citation

The High-Resolution Structure of Activated Opsin Reveals a Conserved Solvent Network in the Transmembrane Region Essential for Activation. Blankenship, E., Vahedi-Faridi, A., Lodowski, D.T. Structure (2015) 23:2358-2364. DOI 10.1016/j.str.2015.09.015 · PubMed

Other PDB entries of the same protein (UniProt P02699 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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