Photosynthetic reaction center from rhodopseudomonas viridis (ubiquinone-2 complex). Determined by X-ray diffraction at 2.45 Å resolution. Released 11 Nov 1998.
Explore 2PRC in 3D Show helices and sheets RCSB PDB PDBe
2PRC contains 91 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 | 39-42 | 4 | |
| α-helix | 52-55 | 4 | |
| α-helix | 67-81 | 15 | |
| α-helix | 86-89 | 4 | |
| β-strand | 92 | 1 | 2 |
| β-strand | 95 | 1 | 2 |
| α-helix | 102-120 | 19 | |
| α-helix | 122-125 | 4 | |
| α-helix | 132-136 | 5 | |
| β-strand | 146 | 1 | 3 |
| α-helix | 159-160 | 2 | |
| 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 | 4 |
| α-helix | 217-219 | 3 | |
| α-helix | 221-222 | 2 | |
| α-helix | 224-239 | 16 | |
| α-helix | 244-246 | 3 | |
| β-strand | 248 | 1 | 5 |
| α-helix | 250-252 | 3 | |
| β-strand | 257 | 1 | 6 |
| β-strand | 260 | 1 | 5 |
| 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 | 3 |
| α-helix | 305-309 | 5 | |
| α-helix | 315-318 | 4 | |
| α-helix | 326-328 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 2 | 1 | 4 |
| β-strand | 5 | 1 | 19 |
| β-strand | 11 | 1 | 19 |
| α-helix | 12-25 | 14 | |
| α-helix | 26-32 | 7 | |
| α-helix | 33-35 | 3 | |
| α-helix | 43 | 1 | |
| β-strand | 44 | 1 | 7 |
| α-helix | 56-60 | 5 | |
| α-helix | 63-65 | 3 | |
| β-strand | 66-69 | 4 | 11 |
| α-helix | 70 | 1 | |
| β-strand | 75-78 | 4 | 11 |
| β-strand | 90-92 | 3 | 8 |
| α-helix | 99-100 | 2 | |
| β-strand | 101-103 | 3 | 8 |
| α-helix | 107-110 | 4 | |
| α-helix | 113-115 | 3 | |
| β-strand | 124 | 1 | 20 |
| β-strand | 126 | 1 | 21 |
| β-strand | 132 | 1 | 21 |
| β-strand | 134-136 | 3 | 13 |
| β-strand | 144-145 | 2 | 14 |
| α-helix | 146 | 1 | |
| β-strand | 147 | 1 | 22 |
| β-strand | 149 | 1 | 22 |
| α-helix | 155 | 1 | |
| β-strand | 156-158 | 3 | 13 |
| β-strand | 164-174 | 11 | 13 |
| β-strand | 179-187 | 9 | 13 |
| β-strand | 193-197 | 5 | 13 |
| α-helix | 198-200 | 3 | |
| β-strand | 202-203 | 2 | 13 |
| β-strand | 208-209 | 2 | 13 |
| α-helix | 215-220 | 6 | |
| β-strand | 231 | 1 | 20 |
| α-helix | 232-248 | 17 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 2 | 1 | 7 |
| α-helix | 7-9 | 3 | |
| β-strand | 11 | 1 | 8 |
| α-helix | 19-22 | 4 | |
| β-strand | 25-26 | 2 | 9 |
| β-strand | 29-30 | 2 | 9 |
| α-helix | 32-55 | 24 | |
| β-strand | 66 | 1 | 10 |
| α-helix | 68-70 | 3 | |
| 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 | 10 |
| α-helix | 152-163 | 12 | |
| α-helix | 167-169 | 3 | |
| α-helix | 171-198 | 28 | |
| α-helix | 204 | 1 | |
| β-strand | 205 | 1 | 11 |
| α-helix | 206 | 1 | |
| α-helix | 209-220 | 12 | |
| α-helix | 226-249 | 24 | |
| β-strand | 251 | 1 | 12 |
| β-strand | 255 | 1 | 12 |
| α-helix | 259-262 | 4 | |
| α-helix | 264-267 | 4 | |
| α-helix | 270-272 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 11 | 1 | 13 |
| β-strand | 12-13 | 2 | 14 |
| α-helix | 15-17 | 3 | |
| α-helix | 19-21 | 3 | |
| α-helix | 25-27 | 3 | |
| β-strand | 28-29 | 2 | 15 |
| β-strand | 33-34 | 2 | 16 |
| α-helix | 38-41 | 4 | |
| β-strand | 45-46 | 2 | 16 |
| β-strand | 49-50 | 2 | 15 |
| α-helix | 53-76 | 24 | |
| α-helix | 81-87 | 7 | |
| α-helix | 88-90 | 3 | |
| β-strand | 93 | 1 | 17 |
| α-helix | 104-106 | 3 | |
| α-helix | 107-109 | 3 | |
| α-helix | 111-138 | 28 | |
| 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 | 17 |
| 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 | 18 |
| β-strand | 289 | 1 | 18 |
| α-helix | 292-299 | 8 | |
| α-helix | 310-311 | 2 | |
| β-strand | 312 | 1 | 6 |
| α-helix | 315-317 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Photosynthetic reaction center | C | protein | 336 | Blastochloris viridis | P07173 (AlphaFold model) |
| Photosynthetic reaction center | L | protein | 273 | Blastochloris viridis | P06009 (AlphaFold model) |
| Photosynthetic reaction center | M | protein | 323 | Blastochloris viridis | P06010 (AlphaFold model) |
| Photosynthetic reaction center | H | protein | 258 | Blastochloris viridis | P06008 (AlphaFold model) |
>2PRC_1 PHOTOSYNTHETIC REACTION CENTER (chains C) CFEPPPATTTQTGFRGLSMGEVLHPATVKAKKERDAQYPPALAAVKAEGPPVSQVYKNVK VLGNLTEAEFLRTMTAITEWVSPQEGCTYCHDENNLASEAKYPYVVARRMLEMTRAINTN WTQHVAQTGVTCYTCHRGTPLPPYVRYLEPTLPLNNRETPTHVERVETRSGYVVRLAKYT AYSALNYDPFTMFLANDKRQVRVVPQTALPLVGVSRGKERRPLSDAYATFALMMSISDSL GTNCTFCHNAQTFESWGKKSTPQRAIAWWGIRMVRDLNMNYLAPLNASLPASRLGRQGEA PQADCRTCHQGVTKPLFGASRLKDYPELGPIKAAAK
>2PRC_2 PHOTOSYNTHETIC REACTION CENTER (chains L) ALLSFERKYRVRGGTLIGGDLFDFWVGPYFVGFFGVSAIFFIFLGVSLIGYAASQGPTWD PFAISINPPDLKYGLGAAPLLEGGFWQAITVCALGAFISWMLREVEISRKLGIGWHVPLA FCVPIFMFCVLQVFRPLLLGSWGHAFPYGILSHLDWVNNFGYQYLNWHYNPGHMSSVSFL FVNAMALGLHGGLILSVANPGDGDKVKTAEHENQYFRDVVGYSIGALSIHRLGLFLASNI FLTGAFGTIASGPFWTRGWPEWWGWWLDIPFWS
>2PRC_3 PHOTOSYNTHETIC REACTION CENTER (chains M) ADYQTIYTQIQARGPHITVSGEWGDNDRVGKPFYSYWLGKIGDAQIGPIYLGASGIAAFA FGSTAILIILFNMAAEVHFDPLQFFRQFFWLGLYPPKAQYGMGIPPLHDGGWWLMAGLFM TLSLGSWWIRVYSRARALGLGTHIAWNFAAAIFFVLCIGCIHPTLVGSWSEGVPFGIWPH IDWLTAFSIRYGNFYYCPWHGFSIGFAYGCGLLFAAHGATILAVARFGGDREIEQITDRG TAVERAALFWRWTIGFNATIESVHRWGWFFSLMVMVSASVGILLTGTFVDNWYLWCVKHG AAPDYPAYLPATPDPASLPGAPK
>2PRC_4 PHOTOSYNTHETIC REACTION CENTER (chains H) MYHGALAQHLDIAQLVWYAQWLVIWTVVLLYLRREDRREGYPLVEPLGLVKLAPEDGQVY ELPYPKTFVLPHGGTVTVPRRRPETRELKLAQTDGFEGAPLQPTGNPLVDAVGPASYAER AEVVDATVDGKAKIVPLRVATDFSIAEGDVDPRGLPVVAADGVEAGTVTDLWVDRSEHYF RYLELSVAGSARTALIPLGFCDVKKDKIVVTSILSEQFANVPRLQSRDQITLREEDKVSA YYAGGLLYATPERAESLL
| ID | Name | Formula | Copies |
|---|---|---|---|
| HEC | Heme C | C34 H36 Fe N4 O4 | 4 |
| BCB | Bacteriochlorophyll B | C55 H72 Mg N4 O6 | 4 |
| BPB | Bacteriopheophytin B | C55 H74 N4 O6 | 2 |
| UQ2 | Ubiquinone-2 | C19 H26 O4 | 1 |
| LDA | Lauryl dimethylamine-N-oxide | C14 H31 N O | 6 |
| FE2 | FE (II) ion | Fe | 1 |
| MQ7 | Menaquinone-7 | C46 H64 O2 | 1 |
| NS5 | 15-cis-1,2-dihydroneurosporene | C40 H60 | 1 |
Water and common crystallization additives (SO4) are not listed.
The coupling of light-induced electron transfer and proton uptake as derived from crystal structures of reaction centres from Rhodopseudomonas viridis modified at the binding site of the secondary quinone, QB. Lancaster, C.R., Michel, H. Structure (1997) 5:1339-1359. DOI 10.1016/S0969-2126(97)00285-2 · 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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