Photosynthetic reaction center from blastochloris viridis. Determined by X-ray diffraction at 2.4 Å resolution. Released 13 Mar 2007.
Explore 2JBL in 3D Show helices and sheets RCSB PDB PDBe
2JBL contains 88 α-helices and 50 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 | 25-36 | 12 | |
| 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 | 159-160 | 2 | |
| 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 | 224-240 | 17 | |
| 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 | 305-309 | 5 | |
| α-helix | 315-318 | 4 | |
| α-helix | 326-328 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 2 | 1 | 5 |
| β-strand | 5-7 | 3 | 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 |
| 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 | 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 | |
| α-helix | 226-250 | 25 | |
| β-strand | 251 | 1 | 18 |
| β-strand | 255 | 1 | 18 |
| 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 | 12-13 | 2 | 15 |
| α-helix | 19-21 | 3 | |
| α-helix | 25-27 | 3 | |
| β-strand | 28-29 | 2 | 19 |
| β-strand | 33-34 | 2 | 20 |
| α-helix | 38-40 | 3 | |
| β-strand | 45-46 | 2 | 20 |
| β-strand | 49-50 | 2 | 19 |
| α-helix | 53-76 | 24 | |
| α-helix | 81-87 | 7 | |
| α-helix | 88-90 | 3 | |
| β-strand | 93 | 1 | 21 |
| α-helix | 104-106 | 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 | 356 | 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) |
>2JBL_1 PHOTOSYNTHETIC REACTION CENTER CYTOCHROME C SUBUNIT (chains C) MKQLIVNSVATVALASLVAGCFEPPPATTTQTGFRGLSMGEVLHPATVKAKKERDAQYPP ALAAVKAEGPPVSQVYKNVKVLGNLTEAEFLRTMTAITEWVSPQEGCTYCHDENNLASEA KYPYVVARRMLEMTRAINTNWTQHVAQTGVTCYTCHRGTPLPPYVRYLEPTLPLNNRETP THVERVETRSGYVVRLAKYTAYSALNYDPFTMFLANDKRQVRVVPQTALPLVGVSRGKER RPLSDAYATFALMMSISDSLGTNCTFCHNAQTFESWGKKSTPQRAIAWWGIRMVRDLNMN YLAPLNASLPASRLGRQGEAPQADCRTCHQGVTKPLFGASRLKDYPELGPIKAAAK
>2JBL_2 REACTION CENTER PROTEIN H CHAIN (chains H) MYHGALAQHLDIAQLVWYAQWLVIWTVVLLYLRREDRREGYPLVEPLGLVKLAPEDGQVY ELPYPKTFVLPHGGTVTVPRRRPETRELKLAQTDGFEGAPLQPTGNPLVDAVGPASYAER AEVVDATVDGKAKIVPLRVATDFSIAEGDVDPRGLPVVAADGVEAGTVTDLWVDRSEHYF RYLELSVAGSARTALIPLGFCDVKKDKIVVTSILSEQFANVPRLQSRDQITLREEDKVSA YYAGGLLYATPERAESLL
>2JBL_3 REACTION CENTER PROTEIN L CHAIN (chains L) ALLSFERKYRVRGGTLIGGDLFDFWVGPYFVGFFGVSAIFFIFLGVSLIGYAASQGPTWD PFAISINPPDLKYGLGAAPLLEGGFWQAITVCALGAFISWMLREVEISRKLGIGWHVPLA FCVPIFMFCVLQVFRPLLLGSWGHAFPYGILSHLDWVNNFGYQYLNWHYNPGHMSSVSFL FVNAMALGLHGGLILSVANPGDGDKVKTAEHENQYFRDVVGYSIGALSIHRLGLFLASNI FLTGAFGTIASGPFWTRGWPEWWGWWLDIPFWS
>2JBL_4 REACTION CENTER PROTEIN M CHAIN (chains M) ADYQTIYTQIQARGPHITVSGEWGDNDRVGKPFYSYWLGKIGDAQIGPIYLGASGIAAFA FGSTAILIILFNMAAEVHFDPLQFFRQFFWLGLYPPKAQYGMGIPPLHDGGWWLMAGLFM TLSLGSWWIRVYSRARALGLGTHIAWNFAAAIFFVLCIGCIHPTLVGSWSEGVPFGIWPH IDWLTAFSIRYGNFYYCPWHGFSIGFAYGCGLLFAAHGATILAVARFGGDREIEQITDRG TAVERAALFWRWTIGFNATIESVHRWGWFFSLMVMVSASVGILLTGTFVDNWYLWCVKHG AAPDYPAYLPATPDPASLPGAPK
| ID | Name | Formula | Copies |
|---|---|---|---|
| HEC | Heme C | C34 H36 Fe N4 O4 | 4 |
| LDA | Lauryl dimethylamine-N-oxide | C14 H31 N O | 6 |
| BCB | Bacteriochlorophyll B | C55 H72 Mg N4 O6 | 4 |
| BPB | Bacteriopheophytin B | C55 H74 N4 O6 | 2 |
| SMA | Stigmatellin a | C30 H42 O7 | 1 |
| FE | FE (III) 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.
A Comparison of Stigmatellin Conformations, Free and Bound to the Photosynthetic Reaction Center and the Cytochrome Bc(1) Complex. Lancaster, C.R.D., Hunte, C., Kelley, J. et al. J Mol Biol (2007) 368:197. DOI 10.1016/J.JMB.2007.02.013 · 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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