(M)L214A mutant of the Rhodobacter sphaeroides Reaction Center. Determined by X-ray diffraction at 2.7 Å resolution. Released 1 May 2013.
Explore 4IN6 in 3D Show helices and sheets RCSB PDB PDBe
4IN6 contains 52 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 | |
| α-helix | 40 | 1 | |
| α-helix | 42 | 1 | |
| β-strand | 43 | 1 | 1 |
| β-strand | 49 | 1 | 1 |
| α-helix | 50 | 1 | |
| α-helix | 57-61 | 5 | |
| β-strand | 62-66 | 5 | 12 |
| β-strand | 71-75 | 5 | 12 |
| β-strand | 87-89 | 3 | 13 |
| β-strand | 98-100 | 3 | 13 |
| α-helix | 104-107 | 4 | |
| α-helix | 110-112 | 3 | |
| α-helix | 121-122 | 2 | |
| β-strand | 123 | 1 | 14 |
| β-strand | 129 | 1 | 14 |
| β-strand | 131-133 | 3 | 15 |
| α-helix | 134-136 | 3 | |
| β-strand | 141-144 | 4 | 7 |
| β-strand | 152-155 | 4 | 15 |
| β-strand | 160-170 | 11 | 15 |
| β-strand | 175-182 | 8 | 15 |
| β-strand | 188-192 | 5 | 15 |
| α-helix | 193-195 | 3 | |
| β-strand | 197-199 | 3 | 15 |
| β-strand | 202-205 | 4 | 15 |
| α-helix | 210-215 | 6 | |
| 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 | 2 |
| β-strand | 29-30 | 2 | 2 |
| α-helix | 32-56 | 25 | |
| β-strand | 66 | 1 | 3 |
| 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 | 3 |
| α-helix | 152-162 | 11 | |
| β-strand | 163 | 1 | 4 |
| β-strand | 165 | 1 | 4 |
| α-helix | 167-169 | 3 | |
| α-helix | 171-198 | 28 | |
| α-helix | 209-220 | 12 | |
| β-strand | 222 | 1 | 5 |
| α-helix | 228-249 | 22 | |
| β-strand | 251 | 1 | 6 |
| β-strand | 255 | 1 | 6 |
| α-helix | 259-262 | 4 | |
| α-helix | 264-267 | 4 | |
| α-helix | 270-273 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 11-13 | 3 | 7 |
| α-helix | 26-28 | 3 | |
| β-strand | 29 | 1 | 8 |
| β-strand | 35 | 1 | 9 |
| α-helix | 37-40 | 4 | |
| β-strand | 46 | 1 | 9 |
| β-strand | 47 | 1 | 5 |
| β-strand | 51 | 1 | 8 |
| α-helix | 54-77 | 24 | |
| α-helix | 82-87 | 6 | |
| β-strand | 94 | 1 | 10 |
| α-helix | 96-98 | 3 | |
| α-helix | 99-101 | 3 | |
| α-helix | 109-111 | 3 | |
| α-helix | 113-138 | 26 | |
| α-helix | 145-158 | 14 | |
| α-helix | 159-163 | 5 | |
| α-helix | 164-168 | 5 | |
| α-helix | 171-173 | 3 | |
| β-strand | 177 | 1 | 10 |
| 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 | 11 |
| β-strand | 291 | 1 | 11 |
| α-helix | 294-299 | 6 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Reaction center protein L chain | L | protein | 281 | Rhodobacter sphaeroides | Q3J1A5 (AlphaFold model) |
| Reaction center protein M chain | M | protein | 302 | Rhodobacter sphaeroides | Q3J1A6 (AlphaFold model) |
| Reaction center protein H chain | H | protein | 266 | Rhodobacter sphaeroides | Q3J170 (AlphaFold model) |
>4IN6_1 Reaction center protein L chain (chains L) ALLSFERKYRVPGGTLVGGNLFDFWVGPFYVGFFGVATFFFAALGIILIAWSAVLQGTWN PQLISVYPPALEYGLGGAPLAKGGLWQIITICATGAFVSWALREVEICRKLGIGYHIPFA FAFAILAYLTLVLFRPVMMGAWGYAFPYGIWTHLDWVSNTGYTYGNFHYNPAHMIAISFF FTNALALALHGALVLSAANPEKGKEMRTPDHEDTFFRDLVGYSIGTLGIHRLGLLLSLSA VFFSALCMIITGTIWFDQWVDWWQWWVKLPWWANIPGGING
>4IN6_2 Reaction center protein M chain (chains M) AEYQNIFSQVQVRGPADLGMTEDVNLANRSGVGPFSTLLGWFGNAQLGPIYLGSLGVLSL FSGLMWFFTIGIWFWYQAGWNPAVFLRDLFFFSLEPPAPEYGLSFAAPLKEGGLWLIASF FMFVAVWSWWGRTYLRAQALGMGKHTAWAFLSAIWLWMVLGFIRPILMGSWSEAVPYGIF SHLDWTNNFSLVHGNLFYNPFHGLSIAFLYGSAALFAMHGATILAVSRFGGERELEQIAD RGTAAERAALFWRWTMGFNATMEGIHRWAIWMAVLVTLTGGIGILLSGTVVDNWYVWGQN HG
>4IN6_3 Reaction center protein H chain (chains H) HHHHHHMVGVTAFGNFDLASLAIYSFWIFLAGLIYYLQTENMREGYPLENEDGTPAANQG PFPLPKPKTFILPHGRGTLTVPGPESEDRPIALARTAVSEGFPHAPTGDPMKDGVGPASW VARRDLPELDGHGHNKIKPMKAAAGFHVSAGKNPIGLPVRGCDLEIAGKVVDIWVDIPEQ MARFLEVELKDGSTRLLPMQMVKVQSNRVHVNALSSDLFAGIPTIKSPTEVTLLEEDKIC GYVAGGLMYAAPKRKSVVAAMLAEYA
| ID | Name | Formula | Copies |
|---|---|---|---|
| BPH | Bacteriopheophytin a | C55 H76 N4 O6 | 2 |
| U10 | Ubiquinone-10 | C59 H90 O4 | 2 |
| BCL | Bacteriochlorophyll a | C55 H74 Mg N4 O6 | 4 |
| HTO | Heptane-1,2,3-triol | C7 H16 O3 | 1 |
| LDA | Lauryl dimethylamine-N-oxide | C14 H31 N O | 3 |
| FE | FE (III) ion | Fe | 1 |
| SPO | Spheroidene | C41 H60 O | 1 |
| PC1 | 1,2-diacyl-sn-glycero-3-phosphocholine | C44 H88 N O8 P | 1 |
| GGD | Nonadec-10-enoic acid 2-[3,4-dihydroxy-6-hydroxymethyl-5-(3,4,5-trihydroxy-6-hy… | C52 H94 O15 | 1 |
| PO4 | Phosphate ion | O4 P | 5 |
| CDL | Cardiolipin | C81 H156 O17 P2 | 1 |
Water and common crystallization additives (GOL) are not listed.
Role of Rhodobacter sphaeroides Photosynthetic Reaction Center Residue M214 in the Composition, Absorbance Properties, and Conformations of HA and BA Cofactors. Saer, R.G., Hardjasa, A., Rosell, F.I. et al. Biochemistry (2013) 52:2206-2217. DOI 10.1021/bi400207m · PubMed
Other PDB entries of the same protein (UniProt Q3J1A5 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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