Photosynthetic reaction center blastochloris viridis (ATCC). Determined by X-ray diffraction at 2.2 Å resolution. Released 22 Mar 2005.
Explore 1VRN in 3D Show helices and sheets RCSB PDB PDBe
1VRN 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 | 1 | |
| 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 | 67-80 | 14 | |
| 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 | 172-177 | 6 | |
| 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 |
| α-helix | 250-252 | 3 | |
| 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 | 306-309 | 4 | |
| α-helix | 315-318 | 4 | |
| α-helix | 326-328 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 2 | 1 | 5 |
| β-strand | 5-6 | 2 | 8 |
| β-strand | 10-11 | 2 | 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 | 100 | 1 | |
| 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 | 193-197 | 5 | 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 | 19-21 | 3 | |
| β-strand | 25-26 | 2 | 16 |
| β-strand | 29-30 | 2 | 16 |
| α-helix | 33-54 | 22 | |
| 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 | 262-284 | 23 | |
| 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 | 332 | Blastochloris viridis | P07173 (AlphaFold model) |
| Reaction center protein H chain | H | protein | 258 | Blastochloris viridis | P06008 (AlphaFold model) |
| Reaction center protein L chain | L | protein | 273 | Blastochloris viridis | P06009 (AlphaFold model) |
| Reaction center protein M chain | M | protein | 323 | Blastochloris viridis | P06010 (AlphaFold model) |
>1VRN_1 Photosynthetic reaction center cytochrome c subunit (chains C) CFEPPPATTTQTGFRGLSMGEVLHPATVKAKKERDAQYPPALAAVKAEGPPVSQVYKNVK VLGNLTEAEFLRTMTAITEWVSPQEGCTYCHDENNLASEAKYPYVVARRMLEMTRAINTN WTQHVAQTGVTCYTCHRGTPLPPYVRYLEPTLPLNNRETPTHVERVETRSGYVVRLAKYT AYSALNYDPFTMFLANDKRQVRVVPQTALPLVGVSRGKERRPLSDAYATFALMMSISDSL GTNCTFCHNAQTFESWGKKSTPQRAIAWWGIRMVRDLNMNYLAPLNASLPASRLGRQGEA PQADCRTCHQGVTKPLFGASRLKDYPELGPIK
>1VRN_2 Reaction center protein H chain (chains H) MYHGALAQHLDIAQLVWYAQWLVIWTVVLLYLRREDRREGYPLVEPLGLVKLAPEDGQVY ELPYPKTFVLPHGGTVTVPRRRPETRELKLAQTDGFEGAPLQPTGNPLVDAVGPASYAER AEVVDATVDGKAKIVPLRVATDFSIAEGDVDPRGLPVVAADGVEAGTVTDLWVDRSEHYF RYLELSVAGSARTALIPLGFCDVKKDKIVVTSILSEQFANVPRLQSRDQITLREEDKVSA YYAGGLLYATPERAESLL
>1VRN_3 Reaction center protein L chain (chains L) ALLSFERKYRVRGGTLIGGDLFDFWVGPYFVGFFGVSAIFFIFLGVSLIGYAASQGPTWD PFAISINPPDLKYGLGAAPLLEGGFWQAITVCALGAFISWMLREVEISRKLGIGWHVPLA FCVPIFMFCVLQVFRPLLLGSWGHAFPYGILSHLDWVNNFGYQYLNWHYNPGHMSSVSFL FVNAMALGLHGGLILSVANPGDGDKVKTAEHENQYFRDVVGYSIGALSIHRLGLFLASNI FLTGAFGTIASGPFWTRGWPEWWGWWLDIPFWS
>1VRN_4 Reaction center protein M chain (chains M) ADYQTIYTQIQARGPHITVSGEWGDNDRVGKPFYSYWLGKIGDAQIGPIYLGASGIAAFA FGSTAILIILFNMAAEVHFDPLQFFRQFFWLGLYPPKAQYGMGIPPLHDGGWWLMAGLFM TLSLGSWWIRVYSRARALGLGTHIAWNFAAAIFFVLCIGCIHPTLVGSWSEGVPFGIWPH IDWLTAFSIRYGNFYYCPWHGFSIGFAYGCGLLFAAHGATILAVARFGGDREIEQITDRG TAVERAALFWRWTIGFNATIESVHRWGWFFSLMVMVSASVGILLTGTFVDNWYLWCVKHG AAPDYPAYLPATPDPASLPGAPK
| ID | Name | Formula | Copies |
|---|---|---|---|
| BPB | Bacteriopheophytin B | C55 H74 N4 O6 | 2 |
| UQ7 | Ubiquinone-7 | C44 H66 O4 | 1 |
| FE2 | FE (II) ion | Fe | 1 |
| BCB | Bacteriochlorophyll B | C55 H72 Mg N4 O6 | 4 |
| LDA | Lauryl dimethylamine-N-oxide | C14 H31 N O | 6 |
| HEC | Heme C | C34 H36 Fe N4 O4 | 4 |
| NS5 | 15-cis-1,2-dihydroneurosporene | C40 H60 | 1 |
| MQ9 | Menaquinone-9 | C56 H80 O2 | 1 |
Water and common crystallization additives (SO4) are not listed.
Cryogenic structure of the photosynthetic reaction center of Blastochloris viridis in the light and dark. Baxter, R.H., Seagle, B.L., Ponomarenko, N. et al. Acta Crystallogr D Biol Crystallogr (2005) 61:605-612. DOI 10.1107/S0907444905005809 · 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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