Photosynthetic reaction center mutant with ala M260 replaced with trp (chain M, A260W). Determined by X-ray diffraction at 2.1 Å resolution. Released 13 Dec 1999.
Explore 1QOV in 3D Show helices and sheets RCSB PDB PDBe
1QOV contains 53 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 | 62-65 | 4 | 2 |
| β-strand | 72-75 | 4 | 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 | 141-144 | 4 | 6 |
| β-strand | 152-154 | 3 | 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 | 203-204 | 2 | 5 |
| α-helix | 210-212 | 3 | |
| α-helix | 217-219 | 3 | |
| 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 | 150-163 | 14 | |
| 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 | |
| α-helix | 270-273 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 11-13 | 3 | 6 |
| α-helix | 16-17 | 2 | |
| 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 | 53-77 | 25 | |
| 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 | 113-138 | 26 | |
| 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 | 262-285 | 24 | |
| β-strand | 287 | 1 | 14 |
| β-strand | 291 | 1 | 14 |
| α-helix | 294-300 | 7 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Photosynthetic reaction center | H | protein | 260 | RHODOBACTER SPHAEROIDES | P0C0Y7 (AlphaFold model) |
| Photosynthetic reaction center | L | protein | 281 | RHODOBACTER SPHAEROIDES | P0C0Y8 (AlphaFold model) |
| Photosynthetic reaction center | M | protein | 307 | RHODOBACTER SPHAEROIDES | P0C0Y9 (AlphaFold model) |
>1QOV_1 PHOTOSYNTHETIC REACTION CENTER (chains H) MVGVTAFGNFDLASLAIYSFWIFLAGLIYYLQTENMREGYPLENEDGTPAANQGPFPLPK PKTFILPHGRGTLTVPGPESEDRPIALARTAVSEGFPHAPTGDPMKDGVGPASWVARRDL PELDGHGHNKIKPMKAAAGFHVSAGKNPIGLPVRGCDLEIAGKVVDIWVDIPEQMARFLE VELKDGSTRLLPMQMVKVQSNRVHVNALSSDLFAGIPTIKSPTEVTLLEEDKICGYVAGG LMYAAPKRKSVVAAMLAEYA
>1QOV_2 PHOTOSYNTHETIC REACTION CENTER (chains L) ALLSFERKYRVPGGTLVGGNLFDFWVGPFYVGFFGVATFFFAALGIILIAWSAVLQGTWN PQLISVYPPALEYGLGGAPLAKGGLWQIITICATGAFVSWALREVEICRKLGIGYHIPFA FAFAILAYLTLVLFRPVMMGAWGYAFPYGIWTHLDWVSNTGYTYGNFHYNPAHMIAISFF FTNALALALHGALVLSAANPEKGKEMRTPDHEDTFFRDLVGYSIGTLGIHRLGLLLSLSA VFFSALCMIITGTIWFDQWVDWWQWWVKLPWWANIPGGING
>1QOV_3 PHOTOSYNTHETIC REACTION CENTER (chains M) AEYQNIFSQVQVRGPADLGMTEDVNLANRSGVGPFSTLLGWFGNAQLGPIYLGSLGVLSL FSGLMWFFTIGIWFWYQAGWNPAVFLRDLFFFSLEPPAPEYGLSFAAPLKEGGLWLIASF FMFVAVWSWWGRTYLRAQALGMGKHTAWAFLSAIWLWMVLGFIRPILMGSWSEAVPYGIF SHLDWTNNFSLVHGNLFYNPFHGLSIAFLYGSALLFAMHGATILAVSRFGGERELEQIAD RGTAAERAALFWRWTMGFNWTMEGIHRWAIWMAVLVTLTGGIGILLSGTVVDNWYVWGQN HGMAPLN
| ID | Name | Formula | Copies |
|---|---|---|---|
| CDL | Cardiolipin | C81 H156 O17 P2 | 1 |
| SPN | Speroidenone | C41 H70 O2 | 1 |
| FE2 | FE (II) ion | Fe | 1 |
| BPH | Bacteriopheophytin a | C55 H76 N4 O6 | 2 |
| U10 | Ubiquinone-10 | C59 H90 O4 | 1 |
| BCL | Bacteriochlorophyll a | C55 H74 Mg N4 O6 | 4 |
Water and common crystallization additives (CL) are not listed.
Structural Details of an Interaction between Cardiolipin and an Integral Membrane Protein. Mcauley, K.E., Fyfe, P.K., Ridge, J.P. et al. Proc Natl Acad Sci U S A (1999) 96:14706. DOI 10.1073/PNAS.96.26.14706 · 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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