Zinc Substituted Reaction Center M(L214H) Variant of Rhodobacter sphaeroides. Determined by X-ray diffraction at 2.85 Å resolution. Released 22 Jan 2014.
Explore 4N7L in 3D Show helices and sheets RCSB PDB PDBe
4N7L contains 50 α-helices and 34 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 | 56-61 | 6 | |
| 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 | 6 |
| α-helix | 151 | 1 | |
| β-strand | 152-155 | 4 | 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 | 203-205 | 3 | 5 |
| α-helix | 210-212 | 3 | |
| α-helix | 217-218 | 2 | |
| α-helix | 227-243 | 17 |
| 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 | 32-55 | 24 | |
| β-strand | 66 | 1 | 8 |
| 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 | 150-162 | 13 | |
| β-strand | 163 | 1 | 9 |
| β-strand | 165 | 1 | 9 |
| α-helix | 167-169 | 3 | |
| α-helix | 171-198 | 28 | |
| α-helix | 204-206 | 3 | |
| α-helix | 209-220 | 12 | |
| α-helix | 228-249 | 22 | |
| β-strand | 251 | 1 | 10 |
| β-strand | 255 | 1 | 10 |
| 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 | 11 |
| β-strand | 35 | 1 | 12 |
| α-helix | 39-41 | 3 | |
| β-strand | 46 | 1 | 12 |
| β-strand | 51 | 1 | 11 |
| α-helix | 54-77 | 24 | |
| α-helix | 82-87 | 6 | |
| β-strand | 94 | 1 | 13 |
| α-helix | 99-101 | 3 | |
| α-helix | 109-111 | 3 | |
| α-helix | 113-140 | 28 | |
| α-helix | 145-158 | 14 | |
| α-helix | 159-163 | 5 | |
| α-helix | 164-168 | 5 | |
| α-helix | 171-173 | 3 | |
| β-strand | 177 | 1 | 13 |
| 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 | 14 |
| β-strand | 291 | 1 | 14 |
| α-helix | 294-299 | 6 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Reaction center protein H chain | H | protein | 241 | Rhodobacter sphaeroides | Q3J170 (AlphaFold model) |
| Reaction center protein L chain | L | protein | 281 | Rhodobacter sphaeroides | Q3J1A5 (AlphaFold model) |
| Reaction center protein M chain | M | protein | 303 | Rhodobacter sphaeroides | Q3J1A6 (AlphaFold model) |
>4N7L_1 Reaction center protein H chain (chains H) DLASLAIYSFWIFLAGLIYYLQTENMREGYPLENEDGTPAANQGPFPLPKPKTFILPHGR GTLTVPGPESEDRPIALARTAVSEGFPHAPTGDPMKDGVGPASWVARRDLPELDGHGHNK IKPMKAAAGFHVSAGKNPIGLPVRGCDLEIAGKVVDIWVDIPEQMARFLEVELKDGSTRL LPMQMVKVQSNRVHVNALSSDLFAGIPTIKSPTEVTLLEEDKICGYVAGGLMYAAPKRKS V
>4N7L_2 Reaction center protein L chain (chains L) ALLSFERKYRVPGGTLVGGNLFDFWVGPFYVGFFGVATFFFAALGIILIAWSAVLQGTWN PQLISVYPPALEYGLGGAPLAKGGLWQIITICATGAFVSWALREVEICRKLGIGYHIPFA FAFAILAYLTLVLFRPVMMGAWGYAFPYGIWTHLDWVSNTGYTYGNFHYNPAHMIAISFF FTNALALALHGALVLSAANPEKGKEMRTPDHEDTFFRDLVGYSIGTLGIHRLGLLLSLSA VFFSALCMIITGTIWFDQWVDWWQWWVKLPWWANIPGGING
>4N7L_3 Reaction center protein M chain (chains M) AEYQNIFSQVQVRGPADLGMTEDVNLANRSGVGPFSTLLGWFGNAQLGPIYLGSLGVLSL FSGLMWFFTIGIWFWYQAGWNPAVFLRDLFFFSLEPPAPEYGLSFAAPLKEGGLWLIASF FMFVAVWSWWGRTYLRAQALGMGKHTAWAFLSAIWLWMVLGFIRPILMGSWSEAVPYGIF SHLDWTNNFSLVHGNLFYNPFHGLSIAFLYGSAHLFAMHGATILAVSRFGGERELEQIAD RGTAAERAALFWRWTMGFNATMEGIHRWAIWMAVLVTLTGGIGILLSGTVVDNWYVWGQN HGM
| ID | Name | Formula | Copies |
|---|---|---|---|
| GGD | Nonadec-10-enoic acid 2-[3,4-dihydroxy-6-hydroxymethyl-5-(3,4,5-trihydroxy-6-hy… | C52 H94 O15 | 1 |
| LDA | Lauryl dimethylamine-N-oxide | C14 H31 N O | 5 |
| U10 | Ubiquinone-10 | C59 H90 O4 | 2 |
| 2GO | (T-4-S)-[(3S,4S,13R,14R,21R,23R,25R)-9-acetyl-14-ethyl-21-(methoxycarbonyl)-4,8… | C55 H74 N4 O6 Zn | 6 |
| PO4 | Phosphate ion | O4 P | 1 |
| HTO | Heptane-1,2,3-triol | C7 H16 O3 | 2 |
| FE | FE (III) ion | Fe | 1 |
| SPO | Spheroidene | C41 H60 O | 1 |
| CDL | Cardiolipin | C81 H156 O17 P2 | 1 |
| PC1 | 1,2-diacyl-sn-glycero-3-phosphocholine | C44 H88 N O8 P | 1 |
Water and common crystallization additives (GOL) are not listed.
Structural and kinetic properties of Rhodobacter sphaeroides photosynthetic reaction centers containing exclusively Zn-coordinated bacteriochlorophyll as bacteriochlorin cofactors. Saer, R.G., Pan, J., Hardjasa, A. et al. Biochim Biophys Acta (2014) 1837:366-374. DOI 10.1016/j.bbabio.2013.11.015 · PubMed
Other PDB entries of the same protein (UniProt Q3J170 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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