1M0M: Bacteriorhodopsin M1 intermediate

Bacteriorhodopsin M1 intermediate at 1.43 a resolution. Determined by X-ray diffraction at 1.43 Å resolution. Released 11 Sept 2002.

Method
X-ray diffraction
Resolution
1.43 Å
Organism
Halobacterium salinarum
Chains
1
Atoms
2,073
Mol. weight
37.24 kDa
Ligands
SQU, LI1, RET
Released
11 Sept 2002

Explore 1M0M in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1M0M contains 10 α-helices and 2 β-strands across 1 chain. 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: 10 helices, 2 β-strands

ElementResiduesLengthSheet
α-helix10-3021
α-helix37-6226
β-strand67-7151
β-strand74-7851
α-helix81-10020
α-helix105-12723
α-helix131-15424
α-helix165-19127
α-helix201-21313
α-helix214-2185
α-helix219-2257
α-helix227-2293

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
BacteriorhodopsinAprotein262Halobacterium salinarumP02945 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>1M0M_1 BACTERIORHODOPSIN (chains A)
MLELLPTAVEGVSQAQITGRPEWIWLALGTALMGLGTLYFLVKGMGVSDPDAKKFYAITT
LVPAIAFTMYLSMLLGYGLTMVPFGGEQNPIYWARYADWLFTTPLLLLDLALLVDADQGT
ILALVGADGIMIGTGLVGALTKVYSYRFVWWAISTAAMLYILYVLFFGFTSKAESMRPEV
ASTFKVLRNVTVVLWSAYPVVWLIGSEGAGIVPLNIETLLFMVLDVSAKVGFGLILLRSR
AIFGEAEAPEPSAGDGAAATSD

Ligands and cofactors

IDNameFormulaCopies
SQU2,10,23-trimethyl-tetracosaneC27 H561
LI11-[2,6,10.14-tetramethyl-hexadecan-16-yl]-2-[2,10,14-trimethylhexadecan-16-yl]g…C42 H86 O313
RETRetinalC20 H28 O1

Primary citation

Crystallographic structure of the retinal and the protein after deprotonation of the Schiff base: the switch in the bacteriorhodopsin photocycle. Lanyi, J., Schobert, B. J Mol Biol (2002) 321:727-737. DOI 10.1016/S0022-2836(02)00682-4 · PubMed

Other PDB entries of the same protein (UniProt P02945 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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