Double mutant A(L172)C/L(L246)C structure of Photosynthetic Reaction Center From Cereibacter sphaeroides strain RV. Determined by X-ray diffraction at 2.45 Å resolution. Released 22 Nov 2023.
Explore 8C87 in 3D Show helices and sheets RCSB PDB PDBe
8C87 contains 52 α-helices and 32 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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 12-34 | 23 | |
| β-strand | 43 | 1 | 1 |
| β-strand | 49 | 1 | 1 |
| α-helix | 50 | 1 | |
| β-strand | 62-66 | 5 | 2 |
| β-strand | 71-75 | 5 | 2 |
| β-strand | 87-89 | 3 | 3 |
| β-strand | 98-100 | 3 | 3 |
| α-helix | 104-107 | 4 | |
| α-helix | 110-112 | 3 | |
| β-strand | 123 | 1 | 4 |
| β-strand | 129 | 1 | 4 |
| β-strand | 131-133 | 3 | 5 |
| α-helix | 134-136 | 3 | |
| β-strand | 141-144 | 4 | 5 |
| β-strand | 152-155 | 4 | 5 |
| β-strand | 160-170 | 11 | 5 |
| α-helix | 171-173 | 3 | |
| β-strand | 175-182 | 8 | 5 |
| β-strand | 188-192 | 5 | 5 |
| α-helix | 193-195 | 3 | |
| β-strand | 197-198 | 2 | 5 |
| β-strand | 203-205 | 3 | 5 |
| α-helix | 210-215 | 6 | |
| α-helix | 217-219 | 3 | |
| α-helix | 227-243 | 17 | |
| α-helix | 245-247 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 2 | 1 | 1 |
| α-helix | 7-9 | 3 | |
| β-strand | 25-26 | 2 | 6 |
| β-strand | 29-30 | 2 | 6 |
| α-helix | 32-56 | 25 | |
| β-strand | 65-66 | 2 | 7 |
| α-helix | 67-70 | 4 | |
| α-helix | 71-73 | 3 | |
| α-helix | 80-84 | 5 | |
| α-helix | 85-111 | 27 | |
| α-helix | 116-129 | 14 | |
| α-helix | 130-134 | 5 | |
| α-helix | 135-139 | 5 | |
| α-helix | 142-144 | 3 | |
| α-helix | 146-147 | 2 | |
| β-strand | 148-149 | 2 | 7 |
| α-helix | 152-161 | 10 | |
| α-helix | 167-169 | 3 | |
| α-helix | 171-198 | 28 | |
| α-helix | 209-220 | 12 | |
| α-helix | 226-249 | 24 | |
| β-strand | 251 | 1 | 8 |
| β-strand | 255 | 1 | 8 |
| α-helix | 261-263 | 3 | |
| α-helix | 264-267 | 4 | |
| α-helix | 270-272 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 11-13 | 3 | 5 |
| α-helix | 16-17 | 2 | |
| α-helix | 26-28 | 3 | |
| β-strand | 29 | 1 | 9 |
| α-helix | 30-32 | 3 | |
| β-strand | 35 | 1 | 10 |
| α-helix | 39-41 | 3 | |
| β-strand | 46 | 1 | 10 |
| β-strand | 51 | 1 | 9 |
| α-helix | 54-77 | 24 | |
| α-helix | 84-87 | 4 | |
| β-strand | 94 | 1 | 11 |
| α-helix | 95-97 | 3 | |
| α-helix | 99-101 | 3 | |
| α-helix | 109-111 | 3 | |
| α-helix | 113-139 | 27 | |
| α-helix | 145-158 | 14 | |
| α-helix | 159-163 | 5 | |
| α-helix | 164-168 | 5 | |
| α-helix | 171-173 | 3 | |
| β-strand | 177 | 1 | 11 |
| α-helix | 179-192 | 14 | |
| α-helix | 196-198 | 3 | |
| α-helix | 200-225 | 26 | |
| α-helix | 227-229 | 3 | |
| α-helix | 234-239 | 6 | |
| α-helix | 243-256 | 14 | |
| α-helix | 264-285 | 22 | |
| β-strand | 287 | 1 | 12 |
| β-strand | 291 | 1 | 12 |
| α-helix | 294-300 | 7 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Reaction center protein H chain | H | protein | 251 | Cereibacter sphaeroides 2.4.1 | Q3J170 (AlphaFold model) |
| Reaction center protein L chain | L | protein | 281 | Cereibacter sphaeroides 2.4.1 | Q3J1A5 (AlphaFold model) |
| Reaction center protein M chain | M | protein | 303 | Cereibacter sphaeroides 2.4.1 | Q3J1A6 (AlphaFold model) |
>8C87_1 Reaction center protein H chain (chains H) FDLASLAIYSFWIFLAGLIYYLQTENMREGYPLENEDGTPAANQGPFPLPKPKTFILPHG RGTLTVPGPESEDRPIALARTAVSEGFPHAPTGDPMKDGVGPASWVARRDLPELDGHGHN KIKPMKAAAGFHVSAGKNPIGLPVRGCDLEIAGKVVDIWVDIPEQMARFLEVELKDGSTR LLPMQMVKVQSNRVHVNALSSDLFAGIPTIKSPTEVTLLEEDKICGYVAGGLMYAAPKRK SVVAAMLAEYA
>8C87_2 Reaction center protein L chain (chains L) ALLSFERKYRVPGGTLVGGNLFDFWVGPFYVGFFGVATFFFAALGIILIAWSAVLQGTWN PQLISVYPPALEYGLGGAPLAKGGLWQIITICATGAFVSWALREVEICRKLGIGYHIPFA FAFAILAYLTLVLFRPVMMGAWGYAFPYGIWTHLDWVSNTGYTYGNFHYNPCHMIAITFF FTNALALALHGALVLSAANPEKGKEMRTPDHEDTFFRDLVGYSIGTLGIHRLGLLLSLSA VFFSACCMIITGTIWFDQWVDWWQWWVKLPWWANIPGGING
>8C87_3 Reaction center protein M chain (chains M) AEYQNIFTQVQVRGPADLGMTEDVNLANRSGVGPFSTLLGWFGNAQLGPIYLGSLGVLSL FSGLMWFFTIGIWFWYQAGWNPAVFLRDLFFFSLEPPAPEYGLSFAAPLKEGGLWLIASF FMFVAVWSWWGRTYLRAQALGMGKHTAWAFLSAIWLWMVLGFIRPILMGSWSEAVPYGIF SHLDWTNNFSLVHGNLFYNPFHGLSIAFLYGSALLFAMHGATILAVSRFGGERELEQIAD RGTAAERAALFWRWTMGFNATMEGIHRWAIWMAVLVTLTGGIGILLSGTVVDNWYVWGQN HGM
| ID | Name | Formula | Copies |
|---|---|---|---|
| BPH | Bacteriopheophytin a | C55 H76 N4 O6 | 2 |
| BCL | Bacteriochlorophyll a | C55 H74 Mg N4 O6 | 4 |
| OLC | (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate | C21 H40 O4 | 1 |
| LDA | Lauryl dimethylamine-N-oxide | C14 H31 N O | 12 |
| SPN | Speroidenone | C41 H70 O2 | 1 |
| U10 | Ubiquinone-10 | C59 H90 O4 | 1 |
| FE | FE (III) ion | Fe | 1 |
| CDL | Cardiolipin | C81 H156 O17 P2 | 1 |
| HTO | Heptane-1,2,3-triol | C7 H16 O3 | 2 |
Water and common crystallization additives (EDO, UNL) are not listed.
Stabilization of Cereibacter sphaeroides Photosynthetic Reaction Center by the Introduction of Disulfide Bonds. Selikhanov, G., Atamas, A., Yukhimchuk, D. et al. Membranes (Basel) (2023) 13. DOI 10.3390/membranes13020154 · PubMed
Other PDB entries of the same protein (UniProt Q3J170 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 8C87 directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.