5LRI: Reaction center protein L chain

Photosynthetic reaction center mutant with GLUL212 replaced with trp (chain L, EL212W). Determined by X-ray diffraction at 2.4 Å resolution. Released 9 Nov 2016.

Method
X-ray diffraction
Resolution
2.4 Å
Organism
Rhodobacter sphaeroides (strain ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158)
Chains
3
Atoms
7,494
Mol. weight
104.67 kDa
Ligands
LDA, FE, DD9, U10
Released
9 Nov 2016

Explore 5LRI in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5LRI contains 53 α-helices and 36 β-strands across 3 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 H: 11 helices, 16 β-strands

ElementResiduesLengthSheet
α-helix12-3423
β-strand4311
β-strand4911
α-helix501
α-helix57-615
β-strand62-65412
β-strand72-75412
β-strand87-89313
β-strand98-100313
α-helix104-1074
α-helix110-1123
β-strand123114
β-strand129114
β-strand131-133315
α-helix134-1363
β-strand141-14447
β-strand152-155415
β-strand160-1701115
β-strand175-182815
β-strand188-192515
α-helix193-1953
β-strand197-198215
β-strand203-205315
α-helix210-2123
α-helix217-2193
α-helix227-24317
α-helix245-2473
Chain L: 20 helices, 10 β-strands
ElementResiduesLengthSheet
β-strand211
α-helix7-93
β-strand25-2622
β-strand29-3022
α-helix32-5625
β-strand6613
α-helix67-704
α-helix71-733
α-helix80-823
α-helix84-11128
α-helix116-12914
α-helix130-1345
α-helix135-1384
α-helix142-1443
α-helix146-1472
β-strand14813
α-helix152-16211
β-strand16314
β-strand16514
α-helix167-1693
α-helix171-19828
α-helix204-2063
α-helix209-22012
β-strand22215
α-helix226-24924
β-strand25116
β-strand25516
α-helix259-2635
α-helix264-2674
α-helix270-2734
Chain M: 22 helices, 10 β-strands
ElementResiduesLengthSheet
β-strand11-1337
α-helix26-283
β-strand2918
β-strand3519
α-helix39-413
β-strand4619
β-strand4715
β-strand5118
α-helix54-7724
α-helix82-876
α-helix89-913
β-strand94110
α-helix95-984
α-helix99-1013
α-helix109-1113
α-helix113-13927
α-helix145-15814
α-helix159-1635
α-helix164-1674
α-helix171-1733
α-helix175-1762
β-strand177110
α-helix179-19214
α-helix196-1983
α-helix200-22526
α-helix227-2293
α-helix234-2396
α-helix243-25614
α-helix264-28522
β-strand287111
β-strand291111
α-helix294-2996

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Reaction center protein L chainLprotein281Rhodobacter sphaeroides (strain ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158)Q3J1A5 (AlphaFold model)
Reaction center protein M chainMprotein307Rhodobacter sphaeroides (strain ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158)Q3J1A6 (AlphaFold model)
Reaction center protein H chainHprotein260Rhodobacter sphaeroides (strain ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158)Q3J170 (AlphaFold model)
Sequence of entity 1 (L), FASTA
>5LRI_1 Reaction center protein L chain (chains L)
ALLSFERKYRVPGGTLVGGNLFDFWVGPFYVGFFGVATFFFAALGIILIAWSAVLQGTWN
PQLISVYPPALEYGLGGAPLAKGGLWQIITICATGAFVSWALREVEICRKLGIGYHIPFA
FAFAILAYLTLVLFRPVMMGAWGYAFPYGIWTHLDWVSNTGYTYGNFHYNPAHMIAISFF
FTNALALALHGALVLSAANPEKGKEMRTPDHWDTFFRDLVGYSIGTLGIHRLGLLLSLSA
VFFSALCMIITGTIWFDQWVDWWQWWVKLPWWANIPGGING
Sequence of entity 2 (M), FASTA
>5LRI_2 Reaction center protein M chain (chains M)
AEYQNIFSQVQVRGPADLGMTEDVNLANRSGVGPFSTLLGWFGNAQLGPIYLGSLGVLSL
FSGLMWFFTIGIWFWYQAGWNPAVFLRDLFFFSLEPPAPEYGLSFAAPLKEGGLWLIASF
FMFVAVWSWWGRTYLRAQALGMGKHTAWAFLSAIWLWMVLGFIRPILMGSWSEAVPYGIF
SHLDWTNNFSLVHGNLFYNPFHGLSIAFLYGSALLFAMHGATILAVSRFGGERELEQIAD
RGTAAERAALFWRWTMGFNATMEGIHRWAIWMAVLVTLTGGIGILLSGTVVDNWYVWGQN
HGMAPLN
Sequence of entity 3 (H), FASTA
>5LRI_3 Reaction center protein H chain (chains H)
MVGVTAFGNFDLASLAIYSFWIFLAGLIYYLQTENMREGYPLENEDGTPAANQGPFPLPK
PKTFILPHGRGTLTVPGPESEDRPIALARTAVSEGFPHAPTGDPMKDGVGPASWVARRDL
PELDGHGHNKIKPMKAAAGFHVSAGKNPIGLPVRGCDLEIAGKVVDIWVDIPEQMARFLE
VELKDGSTRLLPMQMVKVQSNRVHVNALSSDLFAGIPTIKSPTEVTLLEEDKICGYVAGG
LMYAAPKRKSVVAAMLAEYA

Ligands and cofactors

IDNameFormulaCopies
LDALauryl dimethylamine-N-oxideC14 H31 N O5
FEFE (III) ionFe1
DD9nonaneC9 H203
U10Ubiquinone-10C59 H90 O42
BPHBacteriopheophytin aC55 H76 N4 O62
BCLBacteriochlorophyll aC55 H74 Mg N4 O64
CDLCardiolipinC81 H156 O17 P21
SPNSperoidenoneC41 H70 O21

Primary citation

On the mechanism of ubiquinone mediated photocurrent generation by a reaction center based photocathode. Friebe, V.M., Swainsbury, D.J., Fyfe, P.K. et al. Biochim Biophys Acta (2016) 1857:1925-1934. DOI 10.1016/j.bbabio.2016.09.011 · PubMed

Other PDB entries of the same protein (UniProt Q3J1A5 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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