Photosynthetic reaction center mutant with ala M149 replaced with trp (chain M, AM149W). Determined by X-ray diffraction at 2.2 Å resolution. Released 4 Sept 2007.
Explore 2JIY in 3D Show helices and sheets RCSB PDB PDBe
2JIY contains 51 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 | |
| β-strand | 43 | 1 | 1 |
| β-strand | 49 | 1 | 1 |
| α-helix | 50 | 1 | |
| α-helix | 57-61 | 5 | |
| 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 | 141-145 | 5 | 6 |
| 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 | |
| α-helix | 245-247 | 3 |
| 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 | 32-56 | 25 | |
| β-strand | 66 | 1 | 8 |
| α-helix | 67-70 | 4 | |
| 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 | 152-162 | 11 | |
| α-helix | 167-169 | 3 | |
| α-helix | 171-198 | 28 | |
| α-helix | 204-207 | 4 | |
| α-helix | 209-220 | 12 | |
| β-strand | 222 | 1 | 9 |
| α-helix | 226-249 | 24 | |
| 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 | 10-13 | 4 | 6 |
| α-helix | 26-28 | 3 | |
| β-strand | 29 | 1 | 11 |
| β-strand | 35 | 1 | 12 |
| α-helix | 37-40 | 4 | |
| β-strand | 46 | 1 | 12 |
| β-strand | 47 | 1 | 9 |
| β-strand | 51 | 1 | 11 |
| α-helix | 54-77 | 24 | |
| α-helix | 82-87 | 6 | |
| β-strand | 94 | 1 | 13 |
| α-helix | 95-98 | 4 | |
| α-helix | 99-101 | 3 | |
| α-helix | 109-111 | 3 | |
| α-helix | 113-139 | 27 | |
| α-helix | 145-158 | 14 | |
| α-helix | 159-163 | 5 | |
| α-helix | 164-168 | 5 | |
| α-helix | 171-173 | 3 | |
| α-helix | 175-176 | 2 | |
| 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 | 294-298 | 5 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Reaction center protein H chain | H | protein | 260 | RHODOBACTER SPHAEROIDES | P0C0Y7 (AlphaFold model) |
| Reaction center protein L chain | L | protein | 281 | RHODOBACTER SPHAEROIDES | P0C0Y8 (AlphaFold model) |
| Reaction center protein M chain | M | protein | 308 | RHODOBACTER SPHAEROIDES | P0C0Y9 (AlphaFold model) |
>2JIY_1 REACTION CENTER PROTEIN H CHAIN (chains H) MVGVTAFGNFDLASLAIYSFWIFLAGLIYYLQTENMREGYPLENEDGTPAANQGPFPLPK PKTFILPHGRGTLTVPGPESEDRPIALARTAVSEGFPHAPTGDPMKDGVGPASWVARRDL PELDGHGHNKIKPMKAAAGFHVSAGKNPIGLPVRGCDLEIAGKVVDIWVDIPEQMARFLE VELKDGSTRLLPMQMVKVQSNRVHVNALSSDLFAGIPTIKSPTEVTLLEEDKICGYVAGG LMYAAPKRKSVVAAMLAEYA
>2JIY_2 REACTION CENTER PROTEIN L CHAIN (chains L) ALLSFERKYRVPGGTLVGGNLFDFWVGPFYVGFFGVATFFFAALGIILIAWSAVLQGTWN PQLISVYPPALEYGLGGAPLAKGGLWQIITICATGAFVSWALREVEICRKLGIGYHIPFA FAFAILAYLTLVLFRPVMMGAWGYAFPYGIWTHLDWVSNTGYTYGNFHYNPAHMIAISFF FTNALALALHGALVLSAANPEKGKEMRTPDHEDTFFRDLVGYSIGTLGIHRLGLLLSLSA VFFSALCMIITGTIWFDQWVDWWQWWVKLPWWANIPGGING
>2JIY_3 REACTION CENTER PROTEIN M CHAIN (chains M) MAEYQNIFSQVQVRGPADLGMTEDVNLANRSGVGPFSTLLGWFGNAQLGPIYLGSLGVLS LFSGLMWFFTIGIWFWYQAGWNPAVFLRDLFFFSLEPPAPEYGLSFAAPLKEGGLWLIAS FFMFVAVWSWWGRTYLRAQALGMGKHTAWWFLSAIWLWMVLGFIRPILMGSWSEAVPYGI FSHLDWTNNFSLVHGNLFYNPFHGLSIAFLYGSALLFAMHGATILAVSRFGGERELEQIA DRGTAAERAALFWRWTMGFNATMEGIHRWAIWMAVLVTLTGGIGILLSGTVVDNWYVWGQ NHGMAPLN
| ID | Name | Formula | Copies |
|---|---|---|---|
| LDA | Lauryl dimethylamine-N-oxide | C14 H31 N O | 2 |
| BCL | Bacteriochlorophyll a | C55 H74 Mg N4 O6 | 4 |
| BPH | Bacteriopheophytin a | C55 H76 N4 O6 | 1 |
| U10 | Ubiquinone-10 | C59 H90 O4 | 2 |
| CDL | Cardiolipin | C81 H156 O17 P2 | 1 |
| FE | FE (III) ion | Fe | 1 |
| PO4 | Phosphate ion | O4 P | 1 |
| SPN | Speroidenone | C41 H70 O2 | 1 |
| D12 | Dodecane | C12 H26 | 1 |
Water and common crystallization additives (CL) are not listed.
Structural Responses to Cavity-Creating Mutations in an Integral Membrane Protein. Fyfe, P.K., Potter, J.A., Cheng, J. et al. Biochemistry (2007) 46:10461. DOI 10.1021/BI701085W · PubMed
Other PDB entries of the same protein (UniProt P0C0Y7 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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