Crystal structure of Blastochloris viridis heterodimer mutant reaction center. Determined by X-ray diffraction at 2.5 Å resolution. Released 22 Sept 2009.
Explore 3G7F in 3D Show helices and sheets RCSB PDB PDBe
3G7F contains 90 α-helices and 52 β-strands across 4 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 | 4 | 1 | |
| α-helix | 6-7 | 2 | |
| β-strand | 8-9 | 2 | 1 |
| β-strand | 22-23 | 2 | 1 |
| α-helix | 25-35 | 11 | |
| α-helix | 39-44 | 6 | |
| β-strand | 51 | 1 | 2 |
| α-helix | 52-55 | 4 | |
| β-strand | 66 | 1 | 2 |
| α-helix | 67-81 | 15 | |
| α-helix | 87-89 | 3 | |
| β-strand | 92 | 1 | 3 |
| β-strand | 95 | 1 | 3 |
| α-helix | 102-120 | 19 | |
| α-helix | 122-125 | 4 | |
| α-helix | 132-136 | 5 | |
| β-strand | 146 | 1 | 4 |
| α-helix | 159-161 | 3 | |
| α-helix | 169-171 | 3 | |
| α-helix | 172-179 | 8 | |
| α-helix | 189 | 1 | |
| α-helix | 190-194 | 5 | |
| α-helix | 210 | 1 | |
| β-strand | 211 | 1 | 5 |
| α-helix | 217-219 | 3 | |
| α-helix | 221-222 | 2 | |
| α-helix | 224-239 | 16 | |
| α-helix | 244-246 | 3 | |
| β-strand | 248 | 1 | 6 |
| β-strand | 257 | 1 | 7 |
| β-strand | 260 | 1 | 6 |
| α-helix | 262-277 | 16 | |
| α-helix | 278-282 | 5 | |
| α-helix | 283-287 | 5 | |
| α-helix | 291-293 | 3 | |
| α-helix | 299-301 | 3 | |
| β-strand | 302 | 1 | 4 |
| α-helix | 305-309 | 5 | |
| α-helix | 315-318 | 4 | |
| α-helix | 326-328 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 2 | 1 | 5 |
| β-strand | 5 | 1 | 8 |
| α-helix | 7-9 | 3 | |
| β-strand | 11 | 1 | 8 |
| α-helix | 12-25 | 14 | |
| α-helix | 26-32 | 7 | |
| α-helix | 33-35 | 3 | |
| β-strand | 44 | 1 | 9 |
| α-helix | 56-60 | 5 | |
| α-helix | 63-65 | 3 | |
| β-strand | 66-69 | 4 | 10 |
| β-strand | 75-78 | 4 | 10 |
| α-helix | 87-88 | 2 | |
| β-strand | 90-92 | 3 | 11 |
| α-helix | 99-100 | 2 | |
| β-strand | 101-103 | 3 | 11 |
| α-helix | 107-110 | 4 | |
| α-helix | 113-115 | 3 | |
| β-strand | 124 | 1 | 12 |
| β-strand | 126 | 1 | 13 |
| β-strand | 132 | 1 | 13 |
| β-strand | 134-136 | 3 | 14 |
| β-strand | 144-145 | 2 | 15 |
| α-helix | 146 | 1 | |
| β-strand | 156-158 | 3 | 14 |
| β-strand | 164-174 | 11 | 14 |
| β-strand | 179-187 | 9 | 14 |
| β-strand | 192-197 | 6 | 14 |
| α-helix | 198-200 | 3 | |
| β-strand | 202-203 | 2 | 14 |
| β-strand | 208-209 | 2 | 14 |
| α-helix | 215-220 | 6 | |
| α-helix | 222-224 | 3 | |
| β-strand | 231 | 1 | 12 |
| α-helix | 232-248 | 17 | |
| α-helix | 251-254 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 2 | 1 | 9 |
| α-helix | 7-9 | 3 | |
| β-strand | 11 | 1 | 11 |
| α-helix | 19-22 | 4 | |
| β-strand | 25-26 | 2 | 16 |
| β-strand | 29-30 | 2 | 16 |
| α-helix | 32-54 | 23 | |
| β-strand | 66 | 1 | 17 |
| 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 | 17 |
| α-helix | 152-162 | 11 | |
| α-helix | 167-169 | 3 | |
| α-helix | 171-198 | 28 | |
| α-helix | 204-206 | 3 | |
| α-helix | 209-220 | 12 | |
| β-strand | 222 | 1 | 18 |
| α-helix | 226-250 | 25 | |
| β-strand | 251 | 1 | 19 |
| β-strand | 255 | 1 | 19 |
| α-helix | 259-262 | 4 | |
| α-helix | 264-267 | 4 | |
| α-helix | 270-272 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 3-5 | 3 | |
| β-strand | 11 | 1 | 14 |
| β-strand | 12-13 | 2 | 15 |
| α-helix | 15-17 | 3 | |
| α-helix | 19-21 | 3 | |
| α-helix | 25-27 | 3 | |
| β-strand | 28-29 | 2 | 20 |
| β-strand | 33-34 | 2 | 18 |
| α-helix | 38-41 | 4 | |
| β-strand | 45-46 | 2 | 18 |
| β-strand | 49-50 | 2 | 20 |
| α-helix | 52-76 | 25 | |
| α-helix | 81-87 | 7 | |
| α-helix | 88-90 | 3 | |
| β-strand | 93 | 1 | 21 |
| α-helix | 94-96 | 3 | |
| α-helix | 107-109 | 3 | |
| α-helix | 111-137 | 27 | |
| α-helix | 143-156 | 14 | |
| α-helix | 157-161 | 5 | |
| α-helix | 162-166 | 5 | |
| α-helix | 169-171 | 3 | |
| α-helix | 173-174 | 2 | |
| β-strand | 175 | 1 | 21 |
| α-helix | 177-190 | 14 | |
| α-helix | 194-196 | 3 | |
| α-helix | 198-223 | 26 | |
| α-helix | 225-227 | 3 | |
| α-helix | 232-237 | 6 | |
| α-helix | 241-254 | 14 | |
| α-helix | 260-284 | 25 | |
| β-strand | 285 | 1 | 22 |
| β-strand | 289 | 1 | 22 |
| α-helix | 292-298 | 7 | |
| α-helix | 310-311 | 2 | |
| β-strand | 312 | 1 | 7 |
| α-helix | 315-317 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Photosynthetic reaction center cytochrome c subunit | C | protein | 336 | Blastochloris viridis | P07173 (AlphaFold model) |
| Photosynthetic reaction center H subunit | H | protein | 258 | Blastochloris viridis | P06008 (AlphaFold model) |
| Photosynthetic reaction center L subunit | L | protein | 273 | Blastochloris viridis | P06009 (AlphaFold model) |
| Photosynthetic reaction center M subunit | M | protein | 323 | Blastochloris viridis | P06010 (AlphaFold model) |
>3G7F_1 Photosynthetic reaction center cytochrome c subunit (chains C) CFEPPPATTTQTGFRGLSMGEVLHPATVKAKKERDAQYPPALAAVKAEGPPVSQVYKNVK VLGNLTEAEFLRTMTAITEWVSPQEGCTYCHDENNLASEAKYPYVVARRMLEMTRAINTN WTQHVAQTGVTCYTCHRGTPLPPYVRYLEPTLPLNNRETPTHVERVETRSGYVVRLAKYT AYSALNYDPFTMFLANDKRQVRVVPQTALPLVGVSRGKERRPLSDAYATFALMMSISDSL GTNCTFCHNAQTFESWGKKSTPQRAIAWWGIRMVRDLNMNYLAPLNASLPASRLGRQGEA PQADCRTCHQGVTKPLFGASRLKDYPELGPIKAAAK
>3G7F_2 Photosynthetic reaction center H subunit (chains H) MYHGALAQHLDIAQLVWYAQWLVIWTVVLLYLRREDRREGYPLVEPLGLVKLAPEDGQVY ELPYPKTFVLPHGGTVTVPRRRPETRELKLAQTDGFEGAPLQPTGNPLVDAVGPASYAER AEVVDATVDGKAKIVPLRVATDFSIAEGDVDPRGLPVVAADGVEAGTVTDLWVDRSEHYF RYLELSVAGSARTALIPLGFCDVKKDKIVVTSILSDQFANVPRLQSRDQITLREEDKVSA YYAGGLLYATPERAEALL
>3G7F_3 Photosynthetic reaction center L subunit (chains L) ALLSFERKYRVRGGTLIGGDLFDFWVGPYFVGFFGVSAIFFIFLGVSLIGYAASQGPTWD PFAISINPPDLKYGLGAAPLLEGGFWQAITVCALGAFISWMLREVEISRKLGIGWHVPLA FCVPIFMFCVLQVFRPLLLGSWGHAFPYGILSHLDWVNNFGYQYLNWHYNPGHMSSVSFL FVNAMALGLHGGLILSVANPGDGDKVKTAEHENQYFRDVVGYSIGALSIHRLGLFLASNI FLTGAFGTIASGPFWTRGWPEWWGWWLDIPFWS
>3G7F_4 Photosynthetic reaction center M subunit (chains M) ADYQTIYTQIQARGPHITVSGEWGDNDRVGKPFYSYWLGKIGDAQIGPIYLGASGIAAFA FGSTAILIILFNMAAEVHFDPLQFFRQFFWLGLYPPKAQYGMGIPPLHDGGWWLMAGLFM TLSLGSWWIRVYSRARALGLGTHIAWNFAAAIFFVLCIGCIHPTLVGSWSEGVPFGIWPH IDWLTAFSIRYGNFYYCPWLGFSIGFAYGCGLLFAAHGATILAVARFGGDREIEQITDRG TAVERAALFWRWTIGFNATIESVHRWGWFFSLMVMVSASVGILLTGTFVDNWYLWCVKHG AAPDYPAYLPATPDPASLPGAPK
| ID | Name | Formula | Copies |
|---|---|---|---|
| LDA | Lauryl dimethylamine-N-oxide | C14 H31 N O | 4 |
| NS5 | 15-cis-1,2-dihydroneurosporene | C40 H60 | 1 |
| BCB | Bacteriochlorophyll B | C55 H72 Mg N4 O6 | 3 |
| HTO | Heptane-1,2,3-triol | C7 H16 O3 | 5 |
| HEC | Heme C | C34 H36 Fe N4 O4 | 4 |
| MQ9 | Menaquinone-9 | C56 H80 O2 | 1 |
| FE2 | FE (II) ion | Fe | 1 |
| UQ1 | Ubiquinone-1 | C14 H18 O4 | 2 |
| BPB | Bacteriopheophytin B | C55 H74 N4 O6 | 3 |
Water and common crystallization additives (SO4) are not listed.
Structural and spectropotentiometric analysis of Blastochloris viridis heterodimer mutant reaction center. Ponomarenko, N.S., Li, L., Marino, A.R. et al. Biochim Biophys Acta (2009) 1788:1822-1831. DOI 10.1016/j.bbamem.2009.06.006 · PubMed
Other PDB entries of the same protein (UniProt P07173 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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