Photosynthetic Reaction Center From Rhodobacter Sphaeroides strain RV in surfo crystallization. Determined by X-ray diffraction at 2.1 Å resolution. Released 2 Dec 2020.
Explore 6Z02 in 3D Show helices and sheets RCSB PDB PDBe
6Z02 contains 50 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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 12-34 | 23 | |
| β-strand | 43 | 1 | 1 |
| β-strand | 49 | 1 | 1 |
| α-helix | 50 | 1 | |
| α-helix | 57-61 | 5 | |
| β-strand | 62-65 | 4 | 2 |
| β-strand | 72-75 | 4 | 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 | 6 |
| β-strand | 152-154 | 3 | 5 |
| β-strand | 160-170 | 11 | 5 |
| 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 | 203-204 | 2 | 5 |
| α-helix | 210-212 | 3 | |
| 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 | 7 |
| β-strand | 29-30 | 2 | 7 |
| α-helix | 32-54 | 23 | |
| β-strand | 66 | 1 | 8 |
| α-helix | 67-70 | 4 | |
| α-helix | 71-73 | 3 | |
| α-helix | 80-82 | 3 | |
| α-helix | 84-111 | 28 | |
| 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 | 1 | 8 |
| α-helix | 152-162 | 11 | |
| β-strand | 163 | 1 | 9 |
| β-strand | 165 | 1 | 9 |
| α-helix | 167-169 | 3 | |
| α-helix | 171-198 | 28 | |
| α-helix | 209-220 | 12 | |
| β-strand | 222 | 1 | 10 |
| α-helix | 225-249 | 25 | |
| β-strand | 251 | 1 | 11 |
| β-strand | 255 | 1 | 11 |
| α-helix | 259-262 | 4 | |
| α-helix | 264-267 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 11-13 | 3 | 6 |
| α-helix | 26-28 | 3 | |
| β-strand | 29 | 1 | 12 |
| β-strand | 35 | 1 | 13 |
| α-helix | 39-41 | 3 | |
| β-strand | 46 | 1 | 13 |
| β-strand | 47 | 1 | 10 |
| β-strand | 51 | 1 | 12 |
| α-helix | 54-77 | 24 | |
| α-helix | 82-87 | 6 | |
| β-strand | 94 | 1 | 14 |
| α-helix | 95-98 | 4 | |
| 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 | |
| α-helix | 175-176 | 2 | |
| β-strand | 177 | 1 | 14 |
| 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 | 264-286 | 23 | |
| β-strand | 287 | 1 | 15 |
| β-strand | 291 | 1 | 15 |
| α-helix | 294-300 | 7 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Reaction center protein H chain | H | protein | 241 | Rhodobacter sphaeroides | P0C0Y7 (AlphaFold model) |
| Reaction center protein L chain | L | protein | 281 | Rhodobacter sphaeroides | P0C0Y8 (AlphaFold model) |
| Reaction center protein M chain | M | protein | 302 | Rhodobacter sphaeroides | P0C0Y9 (AlphaFold model) |
>6Z02_1 Reaction center protein H chain (chains H) FDLASLAIYSFWIFLAGLIYYLQTENMREGYPLENEDGTPAANQGPFPLPKPKTFILPHG RGTLTVPGPESEDRPIALARTAVSEGFPHAPTGDPMKDGVGPASWVARRDLPELDGHGHN KIKPMKAAAGFHVSAGKNPIGLPVRGCDLEIAGKVVDIWVDIPEQMARFLEVELKDGSTR LLPMQMVKVQSNRVHVNALSSDLFAGIPTIKSPTEVTLLEEDKICGYVAGGLMYAAPKRK S
>6Z02_2 Reaction center protein L chain (chains L) ALLSFERKYRVPGGTLVGGNLFDFWVGPFYVGFFGVATFFFAALGIILIAWSAVLQGTWN PQLISVYPPALEYGLGGAPLAKGGLWQIITICATGAFVSWALREVEICRKLGIGYHIPFA FAFAILAYLTLVLFRPVMMGAWGYAFPYGIWTHLDWVSNTGYTYGNFHYNPAHMIAITFF FTNALALALHGALVLSAANPEKGKEMRTPDHEDTFFRDLVGYSIGTLGIHRLGLLLSLSA VFFSALCMIITGTIWFDQWVDWWQWWVKLPWWANIPGGING
>6Z02_3 Reaction center protein M chain (chains M) AEYQNIFTQVQVRGPADLGMTEDVNLANRSGVGPFSTLLGWFGNAQLGPIYLGSLGVLSL FSGLMWFFTIGIWFWYQAGWNPAVFLRDLFFFSLEPPAPEYGLSFAAPLKEGGLWLIASF FMFVAVWSWWGRTYLRAQALGMGKHTAWAFLSAIWLWMVLGFIRPILMGSWSEAVPYGIF SHLDWTNNFSLVHGNLFYNPFHGLSIAFLYGSALLFAMHGATILAVSRFGGERELEQIAD RGTAAERAALFWRWTMGFNATMEGIHRWAIWMAVLVTLTGGIGILLSGTVVDNWYVWGQN HG
| ID | Name | Formula | Copies |
|---|---|---|---|
| LDA | Lauryl dimethylamine-N-oxide | C14 H31 N O | 7 |
| MYS | Pentadecane | C15 H32 | 3 |
| PO4 | Phosphate ion | O4 P | 3 |
| BCL | Bacteriochlorophyll a | C55 H74 Mg N4 O6 | 4 |
| BPH | Bacteriopheophytin a | C55 H76 N4 O6 | 2 |
| U10 | Ubiquinone-10 | C59 H90 O4 | 2 |
| D10 | Decane | C10 H22 | 1 |
| DIO | 1,4-diethylene dioxide | C4 H8 O2 | 1 |
| FE | FE (III) ion | Fe | 1 |
| SPN | Speroidenone | C41 H70 O2 | 1 |
| CDL | Cardiolipin | C81 H156 O17 P2 | 1 |
| D12 | Dodecane | C12 H26 | 6 |
| HTO | Heptane-1,2,3-triol | C7 H16 O3 | 3 |
Water and common crystallization additives (EDO, NA, K) are not listed.
Novel approaches for the lipid sponge phase crystallization of the Rhodobacter sphaeroides photosynthetic reaction center. Selikhanov, G., Fufina, T., Vasilieva, L. et al. IUCrJ (2020) 7:1084-1091. DOI 10.1107/S2052252520012142 · PubMed
Other PDB entries of the same protein (UniProt P0C0Y7 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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